Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0005776 autophagosome	IBA GO_REF:0000033	ACCEPT	Summary: autophagosome is a core RAB24 autophagy-associated location. Reason: RAB24 localizes to autophagic vacuoles/autophagic compartments and the autophagosome membrane context is directly relevant to its basal autophagic-compartment maturation/clearance role. Supporting Evidence: PMID:26325487 localization of RAB24 to autophagic vacuoles PMID:26325487 maturation and/or clearance of autophagic compartments under nutrient-rich conditions PMID:10660536 Posttranslational geranylgeranylation of Rab24 PMID:26325487 targeting of RAB24 to autophagic compartments
GO:0030139 endocytic vesicle	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: Endocytic-vesicle activity is plausible Rab-effector context but not the core RAB24 PN function; falcon adds RAB24-specific late-endosomal (Rab7/RILP) degradation evidence. Reason: The IBA inference derives from a broad Rab/endocytic-vesicle family context. Beyond the rabenosyn-5 family-recognition data, the falcon deep research surfaces a more RAB24-specific late-endosomal role - RAB24 colocalizes with Rab7/LAMP1 and forms a complex with Rab7/RILP to support endosome-to-lysosome degradation (Amaya 2016). This strengthens an endocytic/late-endosomal context but remains a degradative late-compartment role rather than a defined early endocytic-vesicle trafficking step, so the core RAB24-specific process evidence is still autophagic-compartment maturation/clearance. The underlying Amaya 2016 paper is not in the cache and was not independently verified, so this is retained as non-core rather than promoted. Supporting Evidence: PMID:16034420 Rab GTPases interact with functionally diverse effectors PMID:16034420 rabenosyn-5 can achieve highly selective recognition file:human/RAB24/RAB24-deep-research-falcon.md RAB24 localizes to late endosomal compartments, where it colocalizes with markers such as Rab7 and LAMP1 file:human/RAB24/RAB24-deep-research-falcon.md Forms a complex with Rab7 and RILP on late endosomal membranes
GO:0000421 autophagosome membrane	IEA GO_REF:0000120	ACCEPT	Summary: autophagosome membrane is a core RAB24 autophagy-associated location, supported by immuno-EM on both limiting membranes. Reason: RAB24 localizes to autophagic vacuoles/autophagic compartments and the autophagosome membrane context is directly relevant to its basal autophagic-compartment maturation/clearance role. The falcon deep research adds that immuno-EM places RAB24 on both the inner and outer limiting membranes of autophagosomes/autophagic vacuoles, reinforcing this membrane localization. Supporting Evidence: PMID:26325487 localization of RAB24 to autophagic vacuoles PMID:26325487 maturation and/or clearance of autophagic compartments under nutrient-rich conditions PMID:10660536 Posttranslational geranylgeranylation of Rab24 PMID:26325487 targeting of RAB24 to autophagic compartments file:human/RAB24/RAB24-deep-research-falcon.md RAB24 localizes to both the inner and outer limiting membranes of autophagosomes and autophagic vacuoles
GO:0003924 GTPase activity	IEA GO_REF:0000002	ACCEPT	Summary: GTPase activity is consistent with RAB24 being an atypical Rab-family small GTPase. Reason: RAB24 is a Rab small GTPase; the evidence also cautions that it has unusually low GTP hydrolysis and is predominantly GTP-bound, but this does not negate the Rab GTPase/GTP-binding molecular-function annotation. Supporting Evidence: PMID:10660536 Rab24 exists predominantly in the GTP state PMID:10660536 The low GTPase activity is related to the presence of serine instead of glutamine
GO:0003925 G protein activity	IEA GO_REF:0000120	ACCEPT	Summary: G protein activity is consistent with RAB24 being an atypical Rab-family small GTPase. Reason: RAB24 is a Rab small GTPase; the evidence also cautions that it has unusually low GTP hydrolysis and is predominantly GTP-bound, but this does not negate the Rab GTPase/GTP-binding molecular-function annotation. Supporting Evidence: PMID:10660536 Rab24 exists predominantly in the GTP state PMID:10660536 The low GTPase activity is related to the presence of serine instead of glutamine
GO:0005525 GTP binding	IEA GO_REF:0000002	ACCEPT	Summary: GTP binding is consistent with RAB24 being an atypical Rab-family small GTPase. Reason: RAB24 is a Rab small GTPase; the evidence also cautions that it has unusually low GTP hydrolysis and is predominantly GTP-bound, but this does not negate the Rab GTPase/GTP-binding molecular-function annotation. Supporting Evidence: PMID:10660536 Rab24 exists predominantly in the GTP state PMID:10660536 The low GTPase activity is related to the presence of serine instead of glutamine
GO:0005819 spindle	IEA GO_REF:0000120	KEEP AS NON CORE	Summary: spindle is transferred mouse oocyte/spindle biology and is not the central proteostasis function. Reason: UniProt and GOA support this as by-similarity mouse-oocyte/meiosis context. It may be biologically real in a reproductive setting, but it is secondary to RAB24 basal autophagic-compartment maturation/clearance for the human PN review. Supporting Evidence: file:human/RAB24/RAB24-uniprot.txt Involved in the modulation of meiotic apparatus assembly and meiotic progression during oocyte maturation file:human/RAB24/RAB24-uniprot.txt possibly through regulation of kinetochore-microtubule interaction
GO:0005829 cytosol	IEA GO_REF:0000044	KEEP AS NON CORE	Summary: cytosol is a broad RAB24 localization/context annotation. Reason: RAB24 can be cytosolic and membrane-associated, with perinuclear/autophagic-compartment localization reported by similarity, but these broad terms should not be treated as the core location when autophagosome/autophagosome membrane is available. Supporting Evidence: PMID:10660536 Posttranslational geranylgeranylation of Rab24 PMID:26325487 targeting of RAB24 to autophagic compartments file:human/RAB24/RAB24-uniprot.txt Only about 20% is recovered in the particulate fraction
GO:0016020 membrane	IEA GO_REF:0000044	KEEP AS NON CORE	Summary: membrane is a broad RAB24 localization/context annotation. Reason: RAB24 can be cytosolic and membrane-associated, with perinuclear/autophagic-compartment localization reported by similarity, but these broad terms should not be treated as the core location when autophagosome/autophagosome membrane is available. Supporting Evidence: PMID:10660536 Posttranslational geranylgeranylation of Rab24 PMID:26325487 targeting of RAB24 to autophagic compartments file:human/RAB24/RAB24-uniprot.txt Only about 20% is recovered in the particulate fraction
GO:0048471 perinuclear region of cytoplasm	IEA GO_REF:0000120	KEEP AS NON CORE	Summary: perinuclear region of cytoplasm is a broad RAB24 localization/context annotation. Reason: RAB24 can be cytosolic and membrane-associated, with perinuclear/autophagic-compartment localization reported by similarity, but these broad terms should not be treated as the core location when autophagosome/autophagosome membrane is available. Supporting Evidence: PMID:10660536 Posttranslational geranylgeranylation of Rab24 PMID:26325487 targeting of RAB24 to autophagic compartments file:human/RAB24/RAB24-uniprot.txt Only about 20% is recovered in the particulate fraction
GO:0098588 bounding membrane of organelle	IEA GO_REF:0000117	KEEP AS NON CORE	Summary: bounding membrane of organelle is a broad RAB24 localization/context annotation. Reason: RAB24 can be cytosolic and membrane-associated, with perinuclear/autophagic-compartment localization reported by similarity, but these broad terms should not be treated as the core location when autophagosome/autophagosome membrane is available. Supporting Evidence: PMID:10660536 Posttranslational geranylgeranylation of Rab24 PMID:26325487 targeting of RAB24 to autophagic compartments file:human/RAB24/RAB24-uniprot.txt Only about 20% is recovered in the particulate fraction
GO:0005515 protein binding	IPI PMID:20562859 Network organization of the human autophagy system.	MARK AS OVER ANNOTATED	Summary: Generic protein binding does not describe the actual RAB24 molecular function. Reason: The interaction record may identify a binding partner, but protein binding is uninformative as a GO molecular function. RAB24 should be represented by Rab-family GTPase/GTP-binding activity and, where evidence is specific, autophagic-compartment localization/process terms.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	MARK AS OVER ANNOTATED	Summary: Generic protein binding does not describe the actual RAB24 molecular function. Reason: The interaction record may identify a binding partner, but protein binding is uninformative as a GO molecular function. RAB24 should be represented by Rab-family GTPase/GTP-binding activity and, where evidence is specific, autophagic-compartment localization/process terms.
GO:0005515 protein binding	IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling...	MARK AS OVER ANNOTATED	Summary: Generic protein binding does not describe the actual RAB24 molecular function. Reason: The interaction record may identify a binding partner, but protein binding is uninformative as a GO molecular function. RAB24 should be represented by Rab-family GTPase/GTP-binding activity and, where evidence is specific, autophagic-compartment localization/process terms.
GO:0005515 protein binding	IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce...	MARK AS OVER ANNOTATED	Summary: Generic protein binding does not describe the actual RAB24 molecular function. Reason: The interaction record may identify a binding partner, but protein binding is uninformative as a GO molecular function. RAB24 should be represented by Rab-family GTPase/GTP-binding activity and, where evidence is specific, autophagic-compartment localization/process terms.
GO:0001556 oocyte maturation	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: oocyte maturation is transferred mouse oocyte/spindle biology and is not the central proteostasis function. Reason: UniProt and GOA support this as by-similarity mouse-oocyte/meiosis context. It may be biologically real in a reproductive setting, but it is secondary to RAB24 basal autophagic-compartment maturation/clearance for the human PN review. Supporting Evidence: file:human/RAB24/RAB24-uniprot.txt Involved in the modulation of meiotic apparatus assembly and meiotic progression during oocyte maturation file:human/RAB24/RAB24-uniprot.txt possibly through regulation of kinetochore-microtubule interaction
GO:0005737 cytoplasm	IEA GO_REF:0000120	KEEP AS NON CORE	Summary: cytoplasm is a broad RAB24 localization/context annotation. Reason: RAB24 can be cytosolic and membrane-associated, with perinuclear/autophagic-compartment localization reported by similarity, but these broad terms should not be treated as the core location when autophagosome/autophagosome membrane is available. Supporting Evidence: PMID:10660536 Posttranslational geranylgeranylation of Rab24 PMID:26325487 targeting of RAB24 to autophagic compartments file:human/RAB24/RAB24-uniprot.txt Only about 20% is recovered in the particulate fraction
GO:0005776 autophagosome	IEA GO_REF:0000107	ACCEPT	Summary: autophagosome is a core RAB24 autophagy-associated location. Reason: RAB24 localizes to autophagic vacuoles/autophagic compartments and the autophagosome membrane context is directly relevant to its basal autophagic-compartment maturation/clearance role. Supporting Evidence: PMID:26325487 localization of RAB24 to autophagic vacuoles PMID:26325487 maturation and/or clearance of autophagic compartments under nutrient-rich conditions PMID:10660536 Posttranslational geranylgeranylation of Rab24 PMID:26325487 targeting of RAB24 to autophagic compartments
GO:0006914 autophagy	IEA GO_REF:0000107	MODIFY	Summary: Generic autophagy is too broad for the RAB24-specific evidence. Reason: The RAB24-specific study places the function at maturation and/or clearance of late autophagic compartments under basal nutrient-rich conditions, while formation and short starvation-induced autophagy are not affected. Replace the broad autophagy term with autophagosome maturation. Proposed replacements: autophagosome maturation Supporting Evidence: PMID:26325487 localization of RAB24 to autophagic vacuoles PMID:26325487 maturation and/or clearance of autophagic compartments under nutrient-rich conditions PMID:26325487 Formation of autophagosomes is shown to be unaffected by RAB24-silencing with siRNA
GO:0008608 attachment of spindle microtubules to kinetochore	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: attachment of spindle microtubules to kinetochore is transferred mouse oocyte/spindle biology and is not the central proteostasis function. Reason: UniProt and GOA support this as by-similarity mouse-oocyte/meiosis context. It may be biologically real in a reproductive setting, but it is secondary to RAB24 basal autophagic-compartment maturation/clearance for the human PN review. Supporting Evidence: file:human/RAB24/RAB24-uniprot.txt Involved in the modulation of meiotic apparatus assembly and meiotic progression during oocyte maturation file:human/RAB24/RAB24-uniprot.txt possibly through regulation of kinetochore-microtubule interaction
GO:0140013 meiotic nuclear division	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: meiotic nuclear division is transferred mouse oocyte/spindle biology and is not the central proteostasis function. Reason: UniProt and GOA support this as by-similarity mouse-oocyte/meiosis context. It may be biologically real in a reproductive setting, but it is secondary to RAB24 basal autophagic-compartment maturation/clearance for the human PN review. Supporting Evidence: file:human/RAB24/RAB24-uniprot.txt Involved in the modulation of meiotic apparatus assembly and meiotic progression during oocyte maturation file:human/RAB24/RAB24-uniprot.txt possibly through regulation of kinetochore-microtubule interaction
GO:0005829 cytosol	IDA GO_REF:0000052	KEEP AS NON CORE	Summary: cytosol is a broad RAB24 localization/context annotation. Reason: RAB24 can be cytosolic and membrane-associated, with perinuclear/autophagic-compartment localization reported by similarity, but these broad terms should not be treated as the core location when autophagosome/autophagosome membrane is available. Supporting Evidence: PMID:10660536 Posttranslational geranylgeranylation of Rab24 PMID:26325487 targeting of RAB24 to autophagic compartments file:human/RAB24/RAB24-uniprot.txt Only about 20% is recovered in the particulate fraction
GO:0003925 G protein activity	ISS GO_REF:0000024	ACCEPT	Summary: G protein activity is consistent with RAB24 being an atypical Rab-family small GTPase. Reason: RAB24 is a Rab small GTPase; the evidence also cautions that it has unusually low GTP hydrolysis and is predominantly GTP-bound, but this does not negate the Rab GTPase/GTP-binding molecular-function annotation. Supporting Evidence: PMID:10660536 Rab24 exists predominantly in the GTP state PMID:10660536 The low GTPase activity is related to the presence of serine instead of glutamine
GO:0003924 GTPase activity	ISS GO_REF:0000024	ACCEPT	Summary: GTPase activity is consistent with RAB24 being an atypical Rab-family small GTPase. Reason: RAB24 is a Rab small GTPase; the evidence also cautions that it has unusually low GTP hydrolysis and is predominantly GTP-bound, but this does not negate the Rab GTPase/GTP-binding molecular-function annotation. Supporting Evidence: PMID:10660536 Rab24 exists predominantly in the GTP state PMID:10660536 The low GTPase activity is related to the presence of serine instead of glutamine
GO:0016020 membrane	EXP PMID:10660536 Rab24 is an atypical member of the Rab GTPase family. Defici...	KEEP AS NON CORE	Summary: membrane is a broad RAB24 localization/context annotation. Reason: RAB24 can be cytosolic and membrane-associated, with perinuclear/autophagic-compartment localization reported by similarity, but these broad terms should not be treated as the core location when autophagosome/autophagosome membrane is available. Supporting Evidence: PMID:10660536 Posttranslational geranylgeranylation of Rab24 PMID:26325487 targeting of RAB24 to autophagic compartments file:human/RAB24/RAB24-uniprot.txt Only about 20% is recovered in the particulate fraction
GO:0001556 oocyte maturation	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: oocyte maturation is transferred mouse oocyte/spindle biology and is not the central proteostasis function. Reason: UniProt and GOA support this as by-similarity mouse-oocyte/meiosis context. It may be biologically real in a reproductive setting, but it is secondary to RAB24 basal autophagic-compartment maturation/clearance for the human PN review. Supporting Evidence: file:human/RAB24/RAB24-uniprot.txt Involved in the modulation of meiotic apparatus assembly and meiotic progression during oocyte maturation file:human/RAB24/RAB24-uniprot.txt possibly through regulation of kinetochore-microtubule interaction
GO:0008608 attachment of spindle microtubules to kinetochore	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: attachment of spindle microtubules to kinetochore is transferred mouse oocyte/spindle biology and is not the central proteostasis function. Reason: UniProt and GOA support this as by-similarity mouse-oocyte/meiosis context. It may be biologically real in a reproductive setting, but it is secondary to RAB24 basal autophagic-compartment maturation/clearance for the human PN review. Supporting Evidence: file:human/RAB24/RAB24-uniprot.txt Involved in the modulation of meiotic apparatus assembly and meiotic progression during oocyte maturation file:human/RAB24/RAB24-uniprot.txt possibly through regulation of kinetochore-microtubule interaction
GO:0140013 meiotic nuclear division	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: meiotic nuclear division is transferred mouse oocyte/spindle biology and is not the central proteostasis function. Reason: UniProt and GOA support this as by-similarity mouse-oocyte/meiosis context. It may be biologically real in a reproductive setting, but it is secondary to RAB24 basal autophagic-compartment maturation/clearance for the human PN review. Supporting Evidence: file:human/RAB24/RAB24-uniprot.txt Involved in the modulation of meiotic apparatus assembly and meiotic progression during oocyte maturation file:human/RAB24/RAB24-uniprot.txt possibly through regulation of kinetochore-microtubule interaction
GO:0000421 autophagosome membrane	ISS GO_REF:0000024	ACCEPT	Summary: autophagosome membrane is a core RAB24 autophagy-associated location. Reason: RAB24 localizes to autophagic vacuoles/autophagic compartments and the autophagosome membrane context is directly relevant to its basal autophagic-compartment maturation/clearance role. Supporting Evidence: PMID:26325487 localization of RAB24 to autophagic vacuoles PMID:26325487 maturation and/or clearance of autophagic compartments under nutrient-rich conditions PMID:10660536 Posttranslational geranylgeranylation of Rab24 PMID:26325487 targeting of RAB24 to autophagic compartments
GO:0006914 autophagy	ISS GO_REF:0000024	MODIFY	Summary: Generic autophagy is too broad for the RAB24-specific evidence. Reason: The RAB24-specific study places the function at maturation and/or clearance of late autophagic compartments under basal nutrient-rich conditions, while formation and short starvation-induced autophagy are not affected. Replace the broad autophagy term with autophagosome maturation. Proposed replacements: autophagosome maturation Supporting Evidence: PMID:26325487 localization of RAB24 to autophagic vacuoles PMID:26325487 maturation and/or clearance of autophagic compartments under nutrient-rich conditions PMID:26325487 Formation of autophagosomes is shown to be unaffected by RAB24-silencing with siRNA
GO:0048471 perinuclear region of cytoplasm	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: perinuclear region of cytoplasm is a broad RAB24 localization/context annotation. Reason: RAB24 can be cytosolic and membrane-associated, with perinuclear/autophagic-compartment localization reported by similarity, but these broad terms should not be treated as the core location when autophagosome/autophagosome membrane is available. Supporting Evidence: PMID:10660536 Posttranslational geranylgeranylation of Rab24 PMID:26325487 targeting of RAB24 to autophagic compartments file:human/RAB24/RAB24-uniprot.txt Only about 20% is recovered in the particulate fraction
GO:0005739 mitochondrion	HTP PMID:34800366 Quantitative high-confidence human mitochondrial proteome an...	MARK AS OVER ANNOTATED	Summary: Mitochondrion is not supported as a core RAB24 location. Reason: This high-throughput proteome-derived row does not match the RAB24-specific localization/function evidence, which centers on cytosol, membrane association, and autophagic compartments. Supporting Evidence: file:human/RAB24/RAB24-uniprot.txt Cytoplasm, cytosol PMID:26325487 localization of RAB24 to autophagic vacuoles
GO:0005886 plasma membrane	TAS Reactome:R-HSA-6798743	MARK AS OVER ANNOTATED	Summary: plasma membrane is Reactome degranulation context, not a specific RAB24 core location. Reason: The reviewed RAB24 evidence supports autophagic-compartment/autophagosome membrane localization. Reactome secretory-granule/plasma-membrane context should not be propagated as a core RAB24 cellular-component annotation. Supporting Evidence: PMID:26325487 localization of RAB24 to autophagic vacuoles PMID:26325487 maturation and/or clearance of autophagic compartments under nutrient-rich conditions
GO:0030667 secretory granule membrane	TAS Reactome:R-HSA-6798743	MARK AS OVER ANNOTATED	Summary: secretory granule membrane is Reactome degranulation context, not a specific RAB24 core location. Reason: The reviewed RAB24 evidence supports autophagic-compartment/autophagosome membrane localization. Reactome secretory-granule/plasma-membrane context should not be propagated as a core RAB24 cellular-component annotation. Supporting Evidence: PMID:26325487 localization of RAB24 to autophagic vacuoles PMID:26325487 maturation and/or clearance of autophagic compartments under nutrient-rich conditions
GO:0005515 protein binding	IPI PMID:16034420 Structural basis of family-wide Rab GTPase recognition by ra...	MARK AS OVER ANNOTATED	Summary: Generic protein binding does not describe the actual RAB24 molecular function. Reason: The interaction record may identify a binding partner, but protein binding is uninformative as a GO molecular function. RAB24 should be represented by Rab-family GTPase/GTP-binding activity and, where evidence is specific, autophagic-compartment localization/process terms. Supporting Evidence: PMID:16034420 Rab GTPases interact with functionally diverse effectors PMID:16034420 rabenosyn-5 can achieve highly selective recognition

Core Functions

RAB24 is an atypical Rab-family small GTPase whose GTP-bound state supports targeting to autophagic compartments and late basal autophagic-compartment maturation/clearance.

Molecular Function:

GTPase activity

Directly Involved In:

autophagosome maturation

Cellular Locations:

autophagosome membrane autophagosome

Supporting Evidence:

PMID:10660536
Rab24 exists predominantly in the GTP state
PMID:10660536
The low GTPase activity is related to the presence of serine instead of glutamine
PMID:26325487
localization of RAB24 to autophagic vacuoles
PMID:26325487
maturation and/or clearance of autophagic compartments under nutrient-rich conditions
file:human/RAB24/RAB24-uniprot.txt
RAB24 is required for the clearance of late autophagic vacuoles under basal conditions
file:human/RAB24/RAB24-uniprot.txt
It is not needed for starvation-induced autophagy

RAB24 nucleotide binding is required for its autophagic-compartment targeting, but the protein is atypical because it has weak GTP hydrolysis and remains predominantly GTP-bound.

Molecular Function:

GTP binding

Directly Involved In:

autophagosome maturation

Cellular Locations:

autophagosome membrane

Supporting Evidence:

PMID:10660536
Rab24 exists predominantly in the GTP state
PMID:10660536
The low GTPase activity is related to the presence of serine instead of glutamine
PMID:26325487
guanine nucleotide binding are necessary for the targeting of RAB24 to autophagic compartments

References

GO_REF:0000002

Gene Ontology annotation through association of InterPro records with GO terms

GO_REF:0000024

Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity

GO_REF:0000033

Annotation inferences using phylogenetic trees

GO_REF:0000044

Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt

GO_REF:0000052

Gene Ontology annotation based on curation of immunofluorescence data

GO_REF:0000107

Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara

GO_REF:0000117

Electronic Gene Ontology annotations created by ARBA machine learning models

GO_REF:0000120

Combined Automated Annotation using Multiple IEA Methods

PMID:10660536

Rab24 is an atypical member of the Rab GTPase family. Deficient GTPase activity, GDP dissociation inhibitor interaction, and prenylation of Rab24 expressed in cultured cells.

Human Rab24 is predominantly GTP-bound, has low GTPase activity, is inefficiently prenylated, and is partly membrane-associated.

PMID:16034420

Structural basis of family-wide Rab GTPase recognition by rabenosyn-5.

Rabenosyn-5/ZFYVE20 recognizes Rab GTPases through selective Rab-effector interactions, providing context for the RAB24 interaction but not a specific GO molecular function beyond Rab GTPase activity.

PMID:20562859

Network organization of the human autophagy system.

PMID:32296183

A reference map of the human binary protein interactome.

PMID:33961781

Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.

PMID:34800366

Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.

PMID:35271311

OpenCell: Endogenous tagging for the cartography of human cellular organization.

Reactome:R-HSA-6798743

Exocytosis of secretory granule membrane proteins

file:human/RAB24/RAB24-uniprot.txt

UniProtKB record for human RAB24

UniProt summarizes RAB24 as an atypical Rab protein with low GTPase activity, predominant GTP-bound state, basal late-autophagic-vacuole clearance, and by-similarity oocyte meiotic apparatus context.

file:human/RAB24/RAB24-notes.md

RAB24 review notes

Manual PN-focused curation notes for RAB24; PN no-PMID rows were treated as context only.

PMID:26325487

RAB24 facilitates clearance of autophagic compartments during basal conditions.

RAB24 localizes to autophagic vacuoles/autophagic compartments and supports maturation/clearance of late basal autophagic compartments without affecting autophagosome formation.

file:human/RAB24/RAB24-deep-research-falcon.md

Falcon deep research report for RAB24

LLM-synthesized literature report agreeing that RAB24 is an atypical Rab with low intrinsic GTPase activity, predominantly GTP-bound, prenylation-dependent membrane targeting, and a late-stage basal-autophagy clearance role; it additionally surfaces the Rab7/RILP late-endosomal degradation interaction (Amaya 2016) and immuno-EM localization to both inner and outer autophagic-vacuole membranes.

Suggested Experiments

Experiment: Measure basal autophagic flux and late autophagic-compartment clearance in human RAB24 knockout/rescue cells using wild-type, nucleotide-binding-defective, and prenylation-defective RAB24 variants.

Hypothesis: RAB24 nucleotide binding and membrane targeting are required for late basal autophagic-compartment maturation/clearance.

Experiment: Test whether endogenous human RAB24 is required for autophagosome-lysosome fusion, autolysosome acidification, or post-fusion cargo degradation using LC3/p62 flux reporters and lysosomal inhibitors.

Hypothesis: RAB24 acts late in basal autophagy after autophagosome formation rather than during autophagy induction.

Deep Research

Falcon

(RAB24-deep-research-falcon.md)

Comprehensive Research Report: RAB24 (UniProt Q969Q5) - Functional Annotation Falcon Edison Scientific Literature 23 citations 1 artifacts 2026-06-20T06:22:59.311479

Edison artifact artifact-00 (text/markdown)

The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

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Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

Comprehensive Research Report: RAB24 (UniProt Q969Q5) - Functional Annotation

Gene Identity Verification

RAB24 (UniProt accession Q969Q5) encodes Ras-related protein Rab-24, a small GTPase belonging to the Rab family of the Ras superfamily (homma2021rabfamilyof pages 1-5, ylaanttila2018rolesforrab24 pages 1-3). The gene identity matches the provided UniProt information, confirming RAB24 as a member of the small GTPase superfamily with characteristic Rab family domains (homma2021rabfamilyof pages 1-5). The protein has an approximate molecular mass of 24 kDa and is classified under EC 3.6.5.2 (GTPase activity) (lu2021golgiassociatedrabgtpases pages 4-5).

Primary Protein Function and Enzymatic Activity

GTPase Activity and Catalytic Mechanism

RAB24 functions as a molecular switch that cycles between an active GTP-bound state and an inactive GDP-bound state, catalyzing the hydrolysis of GTP to GDP (homma2021rabfamilyof pages 1-5, xu2024functionandregulation pages 1-3). This nucleotide-dependent cycle is fundamental to Rab protein function and is regulated by guanine nucleotide exchange factors (GEFs), GTPase-activating proteins (GAPs), and GDP dissociation inhibitors (GDIs) (lu2021golgiassociatedrabgtpases pages 1-2, homma2021rabfamilyof pages 1-5).

RAB24 is characterized as an atypical member of the Rab family with distinctive biochemical properties. Unlike typical Rab proteins, RAB24 exhibits unusually low intrinsic GTPase activity and predominantly exists in the GTP-bound state (ylaanttila2018rolesforrab24 pages 1-3, waschbusch2020phosphorylationofrab pages 1-5). This atypical behavior distinguishes RAB24 from other Rab family members and may contribute to its specialized functions in cellular membrane trafficking (ylaanttila2018rolesforrab24 pages 1-3).

Substrate Specificity

As a small GTPase, RAB24 does not have traditional enzymatic substrates in the sense of metabolic enzymes. Rather, its "substrate" is GTP itself, which it hydrolyzes to GDP and inorganic phosphate (homma2021rabfamilyof pages 1-5). The functional specificity of RAB24 is determined by its protein-protein interactions and subcellular localization, which direct it to specific membrane trafficking pathways (xu2024functionandregulation pages 1-3).

Subcellular Localization

RAB24 exhibits dynamic subcellular localization across multiple membrane compartments, which is essential for its diverse functional roles:

Endoplasmic Reticulum and Golgi Apparatus

RAB24 was initially characterized as localizing to the endoplasmic reticulum (ER), ER/cis-Golgi region, and intermediate compartments (lu2021golgiassociatedrabgtpases pages 4-5, ylaanttila2015rab24facilitatesclearance pages 1-2). This localization suggests involvement in early secretory pathway trafficking and ER-Golgi membrane dynamics (ramm2026rab24proteinlevels pages 1-2).

Late Endosomes

RAB24 localizes to late endosomal compartments, where it colocalizes with markers such as Rab7 and LAMP1 (lysosomal-associated membrane protein 1) (amaya2016rab24interactswith pages 1-2). At these sites, RAB24 participates in endosomal maturation and the degradative pathway (amaya2016rab24interactswith pages 1-2).

Autophagic Compartments

Under both basal and starvation-induced autophagy conditions, RAB24 relocalizes to autophagic vacuoles and colocalizes with the autophagosome marker LC3 (microtubule-associated protein 1 light chain 3) (lu2021golgiassociatedrabgtpases pages 4-5, ylaanttila2015rab24facilitatesclearance pages 1-2). Immunoelectron microscopy studies have demonstrated that RAB24 localizes to both the inner and outer limiting membranes of autophagosomes and autophagic vacuoles (ylaanttila2015rab24facilitatesclearance pages 1-2). This dual membrane localization is critical for RAB24's role in autophagosome maturation and clearance.

Membrane Targeting Mechanism

Proper localization of RAB24 to cellular membranes requires post-translational prenylation (geranylgeranylation) at its C-terminal cysteine residues (lu2021golgiassociatedrabgtpases pages 1-2, ylaanttila2015rab24facilitatesclearance pages 1-2). This lipid modification enables RAB24 to anchor to membranes and is essential for its function in autophagy and membrane trafficking (ylaanttila2015rab24facilitatesclearance pages 1-2).

Primary Biological Functions

Autophagy Regulation

The primary and most well-established function of RAB24 is in the regulation of autophagy, specifically in the maturation and clearance of autophagic compartments (ylaanttila2018rolesforrab24 pages 1-3, ylaanttila2015rab24facilitatesclearance pages 1-2).

Basal Autophagy: RAB24 plays a critical role in basal (constitutive) autophagy under nutrient-rich conditions (ylaanttila2015rab24facilitatesclearance pages 1-2). Studies using RAB24 knockdown demonstrate that loss of RAB24 leads to accumulation of late autophagic vacuoles without affecting autophagosome formation, indicating that RAB24 functions primarily in the clearance phase of autophagy rather than in early autophagosome biogenesis (ylaanttila2015rab24facilitatesclearance pages 1-2). This places RAB24 function at the terminal stages of the autophagic process.

Autophagosome Maturation and Fusion: RAB24 facilitates the maturation of autophagosomes and their fusion with lysosomes to form autolysosomes (lu2021golgiassociatedrabgtpases pages 4-5, ylaanttila2018rolesforrab24 pages 1-3). During starvation-induced autophagy, RAB24 relocates to autophagic vacuoles, suggesting dynamic regulation in response to cellular stress (lu2021golgiassociatedrabgtpases pages 4-5).

Aggregate Clearance: RAB24 contributes to the degradation of aggregated proteins, supporting its role in cellular quality control (lu2021golgiassociatedrabgtpases pages 4-5). This function is particularly relevant for maintaining cellular homeostasis and preventing the accumulation of toxic protein aggregates.

Endosomal Trafficking and Degradation

RAB24 functions in the endosome-to-lysosome degradative pathway through its interaction with the Rab7/RILP (Rab-interacting lysosomal protein) complex (amaya2016rab24interactswith pages 1-2). Specifically, RAB24:

Forms a complex with Rab7 and RILP on late endosomal membranes (amaya2016rab24interactswith pages 1-2)
Is required for proper Rab7 membrane recruitment and vesicular localization (amaya2016rab24interactswith pages 1-2)
Regulates endosomal protein degradation, as demonstrated by reduced DQ-BSA degradation in RAB24-depleted cells (amaya2016rab24interactswith pages 1-2)

This endosomal function positions RAB24 as a regulator of cargo degradation in the late stages of the endocytic pathway (amaya2016rab24interactswith pages 1-2).

Vesicular Trafficking

As a member of the Rab GTPase family, RAB24 participates in regulating vesicle formation, transport, tethering, and fusion events between membrane compartments (lu2021golgiassociatedrabgtpases pages 1-2, homma2021rabfamilyof pages 1-5). Its localization to ER, Golgi, and endosomal compartments suggests roles in coordinating membrane trafficking along both secretory and endocytic pathways (ramm2026rab24proteinlevels pages 1-2).

Signaling and Biochemical Pathways

The Autophagic Pathway

RAB24 functions within the macroautophagy pathway, a conserved cellular degradation and recycling system (ylaanttila2018rolesforrab24 pages 1-3). Key aspects include:

Pathway Position: RAB24 acts in the late stages of autophagy, specifically in autophagosome-lysosome fusion and autophagic vacuole clearance, rather than in early autophagosome formation (ylaanttila2015rab24facilitatesclearance pages 1-2). This distinguishes RAB24 from other autophagy-related Rab proteins such as Rab1, Rab5, and Rab33, which function earlier in the pathway (roy2020rabgtpasesin pages 1-3).

Pathway Context: RAB24 is particularly important for basal autophagy (occurring under nutrient-rich conditions) rather than exclusively functioning during starvation-induced autophagy (ylaanttila2015rab24facilitatesclearance pages 1-2). This highlights its role in cellular homeostasis maintenance.

Molecular Interactions: RAB24 colocalizes and functionally interacts with LC3, a core autophagosome marker and component of the LC3 conjugation system essential for autophagosome formation (lu2021golgiassociatedrabgtpases pages 4-5, ylaanttila2015rab24facilitatesclearance pages 1-2, brunel2021autophagyandextracellular pages 1-2).

The Endocytic/Endosomal Pathway

RAB24 participates in the late endocytic pathway through molecular interactions:

Rab7/RILP Complex: RAB24 physically interacts with Rab7 (a master regulator of late endosomal trafficking) and RILP (amaya2016rab24interactswith pages 1-2). RILP functions as a Rab7 effector that recruits dynein/dynactin motor complexes to promote minus-end microtubule transport of late endosomes and lysosomes (amaya2016rab24interactswith pages 1-2).

Functional Role: This interaction network enables RAB24 to influence the trafficking and degradative capacity of late endosomal compartments, affecting cargo delivery to lysosomes (amaya2016rab24interactswith pages 1-2).

Regulation of RAB24 Activity

Post-translational Modifications:

Prenylation: Geranylgeranylation of C-terminal cysteines is required for membrane association and functional localization (lu2021golgiassociatedrabgtpases pages 1-2, ylaanttila2015rab24facilitatesclearance pages 1-2).
Phosphorylation: RAB24 can undergo tyrosine phosphorylation at residues Y17 and/or Y172 (waschbusch2020phosphorylationofrab pages 1-5). Phosphorylation at Y17 may affect the intrinsic GTPase activity of RAB24, providing an additional regulatory mechanism (waschbusch2020phosphorylationofrab pages 1-5).

GTPase Cycle Regulation: While RAB24 exhibits atypically low intrinsic GTPase activity, it is still subject to regulation by GEFs and GAPs, though specific regulators for RAB24 remain incompletely characterized (ylaanttila2018rolesforrab24 pages 1-3).

Tissue-Specific Expression and Distribution

Recent comprehensive analyses of RAB24 protein levels across mouse tissues reveal tissue- and age-specific expression patterns (ramm2026rab24proteinlevels pages 1-2). In adult mice, the highest RAB24 protein levels are found in brain tissue, followed by kidney, with lower levels in pancreas, spleen, liver, lung, heart, and skeletal muscle (ramm2026rab24proteinlevels pages 1-2). Dynamic changes during postnatal development include a sharp increase in brain RAB24 at postnatal day 14, while heart, skeletal muscle, pancreas, and liver show higher levels during the first two postnatal weeks that subsequently decrease (ramm2026rab24proteinlevels pages 1-2).

Immunohistochemical analysis indicates that RAB24 is predominantly expressed in neuronal cells in the brain and in epithelial cells in various tissues (ramm2026rab24proteinlevels pages 1-2). These tissue-specific patterns suggest potential specialized roles for RAB24 in neuronal and epithelial cell maintenance and function.

Disease Associations and Clinical Relevance

Neurodegeneration and Ataxia

RAB24 has emerged as a candidate gene for hereditary ataxia based on studies in canine models. Two missense mutations in RAB24—Q38P in Gordon Setters and Old English Sheepdogs, and G80V in random-bred dogs—cause progressive cerebellar ataxia characterized by Purkinje neuron degeneration, accumulation of autolysosomes, and ubiquitin-protein aggregates (ramm2026rab24proteinlevels pages 1-2, ylaanttila2018rolesforrab24 pages 1-3). These findings implicate defective autophagy as the underlying pathological mechanism and suggest that RAB24 should be considered a candidate gene in human ataxia patients with unclear molecular etiology (ramm2026rab24proteinlevels pages 1-2).

Cancer

RAB24 exhibits context-dependent roles in cancer, functioning as either an oncogenic factor or tumor suppressor depending on tumor type:

Hepatocellular Carcinoma (HCC): RAB24 expression is elevated in HCC tissues compared to normal liver (ramm2026rab24proteinlevels pages 1-2, yang2021roleofrab pages 1-3). Ectopic overexpression of RAB24 enhances malignant phenotypes by promoting cell motility, invasion, adhesion, cell cycle progression, epithelial-to-mesenchymal transition (EMT), and reducing apoptosis (ramm2026rab24proteinlevels pages 1-2). High RAB24 expression serves as an unfavorable prognostic marker in HCC (yang2021roleofrab pages 1-3).

Other Cancers: RAB24 expression patterns vary across cancer types. Elevated RAB24 staining is observed in breast cancer, skin cancer, medulloblastoma, and neuroblastoma compared to normal tissues (ramm2026rab24proteinlevels pages 1-2). Conversely, RAB24 expression is reduced in cancers of the digestive system and urinary tract (ramm2026rab24proteinlevels pages 1-2). In pancreatic adenocarcinoma, RAB24 is reported as an independent low-risk factor, suggesting tumor suppressor activity in this context (ramm2026rab24proteinlevels pages 1-2). High RAB24 expression is an unfavorable prognostic marker in prostate cancer (ramm2026rab24proteinlevels pages 1-2).

Mechanisms: The dual roles of RAB24 in cancer likely reflect tissue-specific differences in autophagy requirements, vesicular trafficking dependencies, and signaling pathway contexts (ji2025theinterrelatedroles pages 1-2, xu2024functionandregulation pages 1-3).

Non-Alcoholic Fatty Liver Disease (NAFLD)

Liver RAB24 levels positively correlate with body fat percentage and are significantly elevated in obese patients with NAFLD (ramm2026rab24proteinlevels pages 1-2). RAB24 knockdown in mouse liver enhances autophagic flux and mitochondrial connectivity while reducing hepatic fat accumulation (ramm2026rab24proteinlevels pages 1-2). These findings link RAB24 to metabolic regulation and lipid homeostasis in the liver.

Bacterial Infections

RAB24 is implicated in host-pathogen interactions during bacterial infections. Certain intracellular pathogens manipulate RAB24-positive compartments to establish replicative niches:

Coxiella burnetii survives and replicates in LC3-positive, RAB24-positive phagolysosomal compartments (lu2021golgiassociatedrabgtpases pages 4-5).
Group A Streptococcus (GAS) infection elicits RAB24-positive autophagosome formation as part of the host xenophagic response (toh2020groupastreptococcus pages 1-3, lu2021golgiassociatedrabgtpases pages 4-5).

These interactions highlight RAB24's role in innate immune responses to intracellular pathogens.

Summary Table

A comprehensive summary of RAB24 characteristics, including protein information, localization, functions, pathways, molecular interactions, post-translational modifications, and disease associations, is provided below:

Category	RAB24 characteristic	Evidence / notes	Citation
Basic protein information	Ras-related protein Rab-24; small GTPase of the Rab family within the Ras superfamily	Reviews describe RAB24 as an atypical Rab-family small GTPase involved in membrane trafficking; Rab proteins generally act as molecular switches cycling between GTP- and GDP-bound states	(homma2021rabfamilyof pages 1-5, ylaanttila2018rolesforrab24 pages 1-3, xu2024functionandregulation pages 1-3)
Basic protein information	Approx. 24 kDa molecular mass	Multiple reviews explicitly refer to “Rab24 GTPase (24 kDa)”	(lu2021golgiassociatedrabgtpases pages 4-5, amaya2016rab24interactswith pages 1-2)
Basic protein information	Enzyme class: small GTPase / guanosine triphosphate hydrolase activity	Rab proteins hydrolyze GTP and are regulated by GEFs/GAPs/GDIs; this applies to RAB24 as a Rab-family member	(homma2021rabfamilyof pages 1-5, waschbusch2020phosphorylationofrab pages 1-5, yang2021roleofrab pages 1-3)
Basic protein information	Atypical Rab with unusually low intrinsic GTPase activity and predominant GTP-bound state reported in earlier work summarized by later reviews	Review of RAB24 biology notes distinctive biochemical features compared with typical Rabs	(ylaanttila2018rolesforrab24 pages 1-3, waschbusch2020phosphorylationofrab pages 1-5)
Subcellular localization	Endoplasmic reticulum and ER/cis-Golgi region	RAB24 was first described at the ER, Golgi, and late endosomes; later reviews summarize localization at ER/cis-Golgi	(ramm2026rab24proteinlevels pages 1-2, lu2021golgiassociatedrabgtpases pages 4-5, ylaanttila2015rab24facilitatesclearance pages 1-2)
Subcellular localization	Late endosomes / lysosome-directed late compartments	Primary work found Rab24 colocalization with Rab7- and LAMP1-positive vesicles and participation in endosome-lysosome degradation	(amaya2016rab24interactswith pages 1-2)
Subcellular localization	Autophagic vacuoles, including LC3-positive autophagic compartments	Under starvation and basal conditions, RAB24 relocalizes to autophagic vacuoles and colocalizes with LC3	(lu2021golgiassociatedrabgtpases pages 4-5, ylaanttila2018rolesforrab24 pages 1-3, ylaanttila2015rab24facilitatesclearance pages 1-2)
Subcellular localization	Inner and outer limiting membranes of autophagic vacuoles	Immuno-EM showed RAB24 on both inner and outer autophagosomal/autophagic vacuole membranes	(ylaanttila2015rab24facilitatesclearance pages 1-2)
Primary molecular functions	Regulator of intracellular membrane trafficking	Rab-family reviews define Rabs as organizers of vesicle biogenesis, transport, tethering, and fusion; RAB24 is one of these membrane-trafficking regulators	(homma2021rabfamilyof pages 1-5, xu2024functionandregulation pages 1-3)
Primary molecular functions	Facilitates clearance/maturation of late autophagic compartments, especially under basal nutrient-rich conditions	RAB24 knockdown increased late autophagic compartments without increasing autophagosome formation, supporting a late-stage clearance role	(ylaanttila2015rab24facilitatesclearance pages 1-2, ylaanttila2018rolesforrab24 pages 1-3)
Primary molecular functions	Promotes endosomal degradative trafficking	Rab24 forms a complex with Rab7/RILP and is required for efficient DQ-BSA degradation and Rab7 membrane recruitment	(amaya2016rab24interactswith pages 1-2)
Key biological processes / pathways	Basal macroautophagy	Reviews and primary work support a specific role in basal autophagy rather than early autophagosome biogenesis	(ylaanttila2018rolesforrab24 pages 1-3, ylaanttila2015rab24facilitatesclearance pages 1-2)
Key biological processes / pathways	Autophagosome maturation / autophagic vacuole clearance	RAB24 is linked to maturation/clearance of degradative autophagic compartments and accumulation of late autophagic vacuoles when absent	(ylaanttila2018rolesforrab24 pages 1-3, ylaanttila2015rab24facilitatesclearance pages 1-2)
Key biological processes / pathways	Endosome-to-lysosome degradative pathway	Rab24 functions with Rab7/RILP on late endosomal membranes in the last steps of endosomal degradation	(amaya2016rab24interactswith pages 1-2)
Key biological processes / pathways	Xenophagy / infection-related autophagy contexts	RAB24 is listed among Rab proteins participating in infection-related autophagy responses, including GAS-targeting autophagy	(toh2020groupastreptococcus pages 1-3, lu2021golgiassociatedrabgtpases pages 4-5)
Molecular interactions	Rab7	Direct interaction reported; Rab24 supports Rab7 association with vesicular membranes in late endosomal degradation	(amaya2016rab24interactswith pages 1-2)
Molecular interactions	RILP (Rab-interacting lysosomal protein)	Rab24 interacts with the Rab7/RILP complex, linking it to dynein-associated late endosomal trafficking	(amaya2016rab24interactswith pages 1-2)
Molecular interactions	LC3 / MAP1LC3-positive autophagic membranes	Colocalization with LC3-positive puncta and autophagic vacuoles is repeatedly observed	(lu2021golgiassociatedrabgtpases pages 4-5, ylaanttila2015rab24facilitatesclearance pages 1-2, brunel2021autophagyandextracellular pages 1-2)
Molecular interactions	Late endosomal/lysosomal markers such as LAMP1	Colocalization with LAMP1-positive compartments supports a late endosomal/lysosomal role	(amaya2016rab24interactswith pages 1-2)
Post-translational modifications	Prenylation at the C-terminus required for membrane targeting	Rab-family reviews explain prenylation-dependent membrane association; RAB24-specific work showed prenylation is necessary for localization to autophagic vacuoles	(lu2021golgiassociatedrabgtpases pages 1-2, ylaanttila2018rolesforrab24 pages 1-3, ylaanttila2015rab24facilitatesclearance pages 1-2)
Post-translational modifications	Tyrosine phosphorylation at Y17 and/or Y172	Review of Rab phosphorylation notes Rab24 phosphorylation at Y17/Y172; Y17 phosphorylation may affect intrinsic GTPase activity	(waschbusch2020phosphorylationofrab pages 1-5)
Disease associations	Neurodegeneration / ataxia	Canine hereditary ataxia-causing RAB24 variants are associated with Purkinje neuron degeneration, autolysosome accumulation, and protein aggregates; authors suggest human relevance	(ramm2026rab24proteinlevels pages 1-2, ylaanttila2018rolesforrab24 pages 1-3)
Disease associations	Hepatocellular carcinoma	Reviews summarize evidence that elevated RAB24 promotes motility, invasion, cell-cycle progression, EMT, and poor prognosis in HCC contexts	(ramm2026rab24proteinlevels pages 1-2, yang2021roleofrab pages 1-3)
Disease associations	Pancreatic adenocarcinoma prognosis	RAB24 has been reported as an independent low-risk/favorable factor in pancreatic adenocarcinoma according to summarized literature	(ramm2026rab24proteinlevels pages 1-2)
Disease associations	Prostate cancer prognosis	High RAB24 expression has been reported as an unfavorable prognostic marker in prostate cancer	(ramm2026rab24proteinlevels pages 1-2)
Disease associations	Fatty liver / NAFLD	Liver RAB24 levels positively correlate with body fat and are elevated in obese patients with NAFLD, according to summarized literature	(ramm2026rab24proteinlevels pages 1-2)
Disease associations	Broad cancer relevance with context-dependent expression	Tissue survey/review data indicate higher RAB24 in some cancers (e.g., breast, skin, pediatric neuronal tumors) and lower in others, implying context-dependent roles	(ramm2026rab24proteinlevels pages 1-2, ji2025theinterrelatedroles pages 1-2, xu2024functionandregulation pages 1-3)

Table: This table summarizes the main experimentally supported and review-supported properties of human RAB24, including its localization, trafficking functions, regulatory features, and disease links. It is useful as a compact evidence map for functional annotation of UniProt Q969Q5.

Recent Research Developments (2023-2024)

Recent literature from 2023-2025 emphasizes RAB24's multifaceted roles:

Cancer Progression: Systematic reviews highlight RAB24 among Rab family proteins with context-dependent oncogenic or tumor suppressor functions, emphasizing its involvement in vesicular trafficking, tumor microenvironment regulation, autophagy, and drug resistance (ji2025theinterrelatedroles pages 1-2).
Autophagy Regulation: Updated reviews on Rab GTPases in autophagy confirm RAB24's role in autophagosome maturation alongside other Golgi-associated Rabs (lu2021golgiassociatedrabgtpases pages 1-2, lu2021golgiassociatedrabgtpases pages 4-5).
Therapeutic Potential: RAB24 is discussed as a potential therapeutic target in hepatocellular carcinoma and metabolic liver disease, with suggestions that modulating RAB24 expression or activity could influence disease progression (yang2021roleofrab pages 1-3).
Protein Expression Patterns: Comprehensive tissue surveys provide the first detailed characterization of RAB24 protein levels across multiple tissues and developmental stages, revealing dynamic regulation and suggesting tissue-specific functional requirements (ramm2026rab24proteinlevels pages 1-2).

Conclusions

RAB24 (UniProt Q969Q5) is a small GTPase belonging to the Rab family that functions as a regulator of membrane trafficking with primary roles in autophagy and endosomal degradation pathways. As an enzyme, RAB24 catalyzes GTP hydrolysis (EC 3.6.5.2), though it exhibits atypically low intrinsic GTPase activity compared to other Rab proteins and predominantly exists in the GTP-bound active state.

The protein localizes to multiple subcellular compartments including the endoplasmic reticulum, cis-Golgi, late endosomes, and autophagic vacuoles. RAB24's primary function is to facilitate the clearance and maturation of autophagic compartments, particularly under basal conditions, and to regulate endosomal protein degradation through interactions with the Rab7/RILP complex. Proper function requires C-terminal prenylation for membrane targeting and can be further regulated by tyrosine phosphorylation.

RAB24 participates in key cellular pathways including macroautophagy (specifically in autophagosome-lysosome fusion and vacuole clearance) and the late endocytic/endosomal degradative pathway. Evidence from both experimental models and human tissue analyses links RAB24 dysfunction to multiple diseases including hereditary ataxia, various cancers (with context-dependent oncogenic or tumor suppressor roles), non-alcoholic fatty liver disease, and bacterial infections.

The accumulated evidence positions RAB24 as an important regulator of cellular homeostasis through its control of protein and organelle quality control mechanisms, with significant implications for neurological health, cancer biology, and metabolic regulation.

References

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Artifacts

Edison artifact artifact-00

Citations

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📚 Additional Documentation

Notes

(RAB24-notes.md)

RAB24 notes

RAB24 is reviewed in the PN autophagosome maturation / lysosome fusion neighborhood. The PN source row has no PMID and is a no-mapping/context-only entry, so it was used to focus the literature search rather than as evidence for any GO action.

Core RAB24 evidence supports an atypical Rab-family small GTPase linked to basal autophagy. UniProt summarizes RAB24 as an atypical Rab with low GTPase activity that is predominantly GTP-bound and says it is "required for the clearance of late autophagic vacuoles under basal conditions" and "not needed for starvation-induced autophagy" [file:human/RAB24/RAB24-uniprot.txt, "RAB24 is required for the clearance of late autophagic vacuoles under basal conditions"; file:human/RAB24/RAB24-uniprot.txt, "It is not needed for starvation-induced autophagy"]. The main autophagy paper confirms "localization of RAB24 to autophagic vacuoles" and shows that RAB24 functions in "maturation and/or clearance of autophagic compartments under nutrient-rich conditions" [PMID:26325487, "localization of RAB24 to autophagic vacuoles"; PMID:26325487, "maturation and/or clearance of autophagic compartments under nutrient-rich conditions"].

The original human biochemical/localization paper supports the generic membrane and atypical Rab-GTPase context but not a precise process term. It reports that Rab24 "exists predominantly in the GTP state" and that inefficient geranylgeranylation/GDI interaction may mean it operates by a "novel mechanism that does not depend on GTP hydrolysis or GDP dissociation inhibitor-mediated recycling" [PMID:10660536, "Rab24 exists predominantly in the GTP state"; PMID:10660536, "does not depend on GTP hydrolysis or GDP dissociation inhibitor-mediated recycling"]. UniProt also notes that only about 20% partitions with membranes and that Rab24 localizes to limiting membranes of autophagic compartments by similarity [file:human/RAB24/RAB24-uniprot.txt, "Only about 20% is recovered in the particulate fraction"; file:human/RAB24/RAB24-uniprot.txt, "limiting membranes of autophagic compartments under basal conditions"].

The rabenosyn-5/ZFYVE20 interaction is real Rab-effector context but does not justify a standalone protein binding GO annotation as a core molecular function. The paper is about Rab-effector recognition specificity, noting that Rab GTPases interact with diverse effectors after nucleotide exchange and that rabenosyn-5 domains selectively recognize Rab subsets [PMID:16034420, "Rab GTPases interact with functionally diverse effectors"; PMID:16034420, "rabenosyn-5 can achieve highly selective recognition"].

The oocyte maturation, spindle, and kinetochore-microtubule annotations are transferred from mouse/by-similarity sources. They may represent a secondary reproductive/cell-division context, but they are not the central human proteostasis function and should not be treated as core for this PN review.

Curation decisions:
- Accept Rab-family GTPase/GTP-binding activity and the specific autophagosome/autophagosome-membrane localization rows.
- Modify generic GO:0006914 autophagy rows to GO:0097352 autophagosome maturation, because the RAB24-specific evidence places the function at late maturation/clearance of basal autophagic compartments rather than general autophagy induction.
- Keep broad cytosol/membrane/perinuclear and endocytic-vesicle locations as non-core context.
- Keep mouse-oocyte and spindle/kinetochore annotations as non-core transferred biology.
- Mark generic protein binding, mitochondrial, plasma-membrane, and secretory-granule membrane rows as over-annotated for the core RAB24 review.

Description cleanup note

The YAML description field was revised to keep it as a standalone biological summary. Project-specific curation framing moved here instead.

Moved out of the YAML description: the prior wording described the late basal autophagy role as PN-related and treated broader cytosolic, membrane, endocytic, and mouse-oocyte/spindle annotations as secondary to the core PN function.

Pn Notes

(RAB24-pn-notes.md)

RAB24 PN Consistency Notes

Generated: 2026-06-18
Project: PROTEOSTASIS
Scope: PN consistency rereview against local AIGR review and available deep-research artifacts
UniProt: Q969Q5
AIGR review status: COMPLETE
Review batch: proteostasis-pr-1217 (PR 1217)
Batch change status: added

Source Files Checked

AIGR review YAML: present - genes/human/RAB24/RAB24-ai-review.yaml
AIGR review HTML: present - genes/human/RAB24/RAB24-ai-review.html
Gene notes: present - genes/human/RAB24/RAB24-notes.md
GOA TSV: present - genes/human/RAB24/RAB24-goa.tsv
UniProt record: present - genes/human/RAB24/RAB24-uniprot.txt
PN dossier: projects/PROTEOSTASIS/reports/phase1_dossiers/RAB24.md
PN consistency section: projects/PROTEOSTASIS/reports/phase1_dossiers/_sections/RAB24.md
PN projection report: projects/PROTEOSTASIS/reports/pn_projection/pn_projected_gene_go_summary.tsv
PN mapping audit: projects/PROTEOSTASIS/reports/pn_mapping_audit/current_mapping_scrutiny.tsv

Deep Research Files

No *-deep-research*.md file found in this gene directory.

AIGR Review Snapshot

Description: RAB24 encodes an atypical Rab-family small GTPase that is predominantly GTP-bound and has low intrinsic GTPase activity. Its best-supported protein-homeostasis role is at late basal autophagy: RAB24 targets to autophagic vacuoles/autophagosome membranes and is required for maturation and/or clearance of late autophagic compartments under nutrient-rich basal conditions, without being required for short starvation-induced autophagosome formation. Broader cytosolic, membrane, endocytic, and mouse-oocyte/spindle annotations are secondary contexts rather than the core RAB24 function.
Existing/core annotation action counts: ACCEPT: 9; KEEP_AS_NON_CORE: 16; MARK_AS_OVER_ANNOTATED: 8; MODIFY: 2

PN Consistency Summary

Consistency: Consistent. Notes, review, and PN agree RAB24 is an atypical, predominantly GTP-bound Rab acting in late/basal autophagic-compartment maturation/clearance (PMID:26325487), not in starvation-induced formation. PN explicitly flags the leaf as "function unknown" and no-mapping; review used it as context only. No contradictions.
PN story / NEW pressure: None. PN makes no positive functional assertion (residual "unknown" node, no projected GO). Review independently MODIFYs generic GO:0006914 autophagy → GO:0097352 autophagosome maturation based on primary evidence — finer than anything PN asserts. Verdict: already captured / PN adds no pressure.
Evidence alignment: Minimal overlap. PN cites one review ("Membrane Trafficking in Autophagy"); review uses primary PMID:26325487, 10660536 (atypical Rab biochem), 16034420 (rabenosyn-5). Several generic protein-binding IPI rows (interactome papers) marked over-annotated; HTP mitochondrion and Reactome secretory-granule rows marked over-annotated — reasonable.
Verdict: Consistent; PN "unknown/no-mapping" placement is honest and the review supplies the specific autophagosome-maturation call. No NEW pressure, mapping correct. No edits required.

Full Consistency Review

UniProt: Q969Q5 · batch: proteostasis-pr-1217 · review status: COMPLETE
PN placement: ALP|Autophagosome closure maturation and lysosome fusion|Specific function in autophagosome maturation and lysosome fusion unknown ; PN-node mapping: group = no_mapping (unknown/residual category, no GO-mappable shared function); class = context_only, too_broad_to_propagate → GO:0016236 macroautophagy; branch = no_mapping. No GO projected.
Consistency: Consistent. Notes, review, and PN agree RAB24 is an atypical, predominantly GTP-bound Rab acting in late/basal autophagic-compartment maturation/clearance (PMID:26325487), not in starvation-induced formation. PN explicitly flags the leaf as "function unknown" and no-mapping; review used it as context only. No contradictions.
PN story / NEW pressure: None. PN makes no positive functional assertion (residual "unknown" node, no projected GO). Review independently MODIFYs generic GO:0006914 autophagy → GO:0097352 autophagosome maturation based on primary evidence — finer than anything PN asserts. Verdict: already captured / PN adds no pressure.
Mapping strategy: This gene does not change the node. no_mapping is appropriate for a residual "unknown" category; the review's GO:0097352 is far narrower than the class-level context GO:0016236 and is correctly derived from the paper, not from node propagation. Good restraint — projecting macroautophagy here would over-annotate (TRAPP precedent).
Evidence alignment: Minimal overlap. PN cites one review ("Membrane Trafficking in Autophagy"); review uses primary PMID:26325487, 10660536 (atypical Rab biochem), 16034420 (rabenosyn-5). Several generic protein-binding IPI rows (interactome papers) marked over-annotated; HTP mitochondrion and Reactome secretory-granule rows marked over-annotated — reasonable.
Verdict: Consistent; PN "unknown/no-mapping" placement is honest and the review supplies the specific autophagosome-maturation call. No NEW pressure, mapping correct. No edits required.

PN Dossier Context

review_batch: proteostasis-pr-1217
review_yaml: genes/human/RAB24/RAB24-ai-review.yaml
PN workbook rows: 1

PN row 1: Autophagy-Lysosome Pathway | Autophagosome closure maturation and lysosome fusion | Specific function in autophagosome maturation and lysosome fusion unknown

UniProt: Q969Q5
In branches: ALP
Notes: Necessary for maturation and clearance of autophagic structures in basal autophagy.
PN references (titles):
- Membrane Trafficking in Autophagy - ScienceDirect
PN-node mapping records (path + ancestors):
- [group] Autophagy-Lysosome Pathway|Autophagosome closure maturation and lysosome fusion|Specific function in autophagosome maturation and lysosome fusion unknown
  status=no_mapping scope= GO=[]
  rationale: Reviewed as an unknown or residual PN category. The label does not provide a shared GO-mappable biological process, molecular function, or cellular component.
- [class] Autophagy-Lysosome Pathway|Autophagosome closure maturation and lysosome fusion
  status=context_only scope=too_broad_to_propagate GO=[GO:0016236 macroautophagy]
  rationale: This class is a late macroautophagy context, but the subtree mixes docking, fusion, localization, membrane-composition, and unknown late-stage roles. The class-level relation is useful for display while propagation is restricted to narrower mechanism nodes.
- [branch] Autophagy-Lysosome Pathway
  status=no_mapping scope= GO=[]
  rationale: Reviewed as the top-level PN branch. It is a project taxonomy umbrella rather than a direct GO assertion; all propagation must come from manually curated child nodes.

Note

This file is generated from the current PROTEOSTASIS phase-1 dossier and local gene-review artifacts. Edit the source review, PN mapping, or dossier rather than this generated note when correcting the underlying curation.

📄 View Raw YAML

id: Q969Q5
gene_symbol: RAB24
product_type: PROTEIN
status: COMPLETE
taxon:
  id: NCBITaxon:9606
  label: Homo sapiens
description: >-
  RAB24 encodes an atypical Rab-family small GTPase that is predominantly GTP-bound and has low
  intrinsic GTPase activity. Its best-supported protein-homeostasis role is at late basal autophagy:
  RAB24 targets to autophagic vacuoles/autophagosome membranes and is required for maturation and/or
  clearance of late autophagic compartments under nutrient-rich basal conditions, without being
  required for short starvation-induced autophagosome formation. Broader cytosolic, membrane,
  endocytic, and mouse-oocyte/spindle annotations are secondary contexts rather than the core RAB24
  function.
existing_annotations:
- term:
    id: GO:0005776
    label: autophagosome
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: is_active_in
  review:
    summary: autophagosome is a core RAB24 autophagy-associated location.
    action: ACCEPT
    reason: RAB24 localizes to autophagic vacuoles/autophagic compartments and the autophagosome membrane context is directly relevant to its basal autophagic-compartment maturation/clearance role.
    supported_by:
    - reference_id: PMID:26325487
      supporting_text: localization of RAB24 to autophagic vacuoles
    - reference_id: PMID:26325487
      supporting_text: maturation and/or clearance of autophagic compartments under nutrient-rich conditions
    - reference_id: PMID:10660536
      supporting_text: Posttranslational geranylgeranylation of Rab24
    - reference_id: PMID:26325487
      supporting_text: targeting of RAB24 to autophagic compartments
- term:
    id: GO:0030139
    label: endocytic vesicle
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: is_active_in
  review:
    summary: Endocytic-vesicle activity is plausible Rab-effector context but not the core RAB24 PN function; falcon adds RAB24-specific late-endosomal (Rab7/RILP) degradation evidence.
    action: KEEP_AS_NON_CORE
    reason: The IBA inference derives from a broad Rab/endocytic-vesicle family context. Beyond the rabenosyn-5 family-recognition data, the falcon deep research surfaces a more RAB24-specific late-endosomal role - RAB24 colocalizes with Rab7/LAMP1 and forms a complex with Rab7/RILP to support endosome-to-lysosome degradation (Amaya 2016). This strengthens an endocytic/late-endosomal context but remains a degradative late-compartment role rather than a defined early endocytic-vesicle trafficking step, so the core RAB24-specific process evidence is still autophagic-compartment maturation/clearance. The underlying Amaya 2016 paper is not in the cache and was not independently verified, so this is retained as non-core rather than promoted.
    supported_by:
    - reference_id: PMID:16034420
      supporting_text: Rab GTPases interact with functionally diverse effectors
    - reference_id: PMID:16034420
      supporting_text: rabenosyn-5 can achieve highly selective recognition
    - reference_id: file:human/RAB24/RAB24-deep-research-falcon.md
      supporting_text: RAB24 localizes to late endosomal compartments, where it colocalizes with markers such as Rab7 and LAMP1
    - reference_id: file:human/RAB24/RAB24-deep-research-falcon.md
      supporting_text: Forms a complex with Rab7 and RILP on late endosomal membranes
- term:
    id: GO:0000421
    label: autophagosome membrane
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: located_in
  review:
    summary: autophagosome membrane is a core RAB24 autophagy-associated location, supported by immuno-EM on both limiting membranes.
    action: ACCEPT
    reason: RAB24 localizes to autophagic vacuoles/autophagic compartments and the autophagosome membrane context is directly relevant to its basal autophagic-compartment maturation/clearance role. The falcon deep research adds that immuno-EM places RAB24 on both the inner and outer limiting membranes of autophagosomes/autophagic vacuoles, reinforcing this membrane localization.
    supported_by:
    - reference_id: PMID:26325487
      supporting_text: localization of RAB24 to autophagic vacuoles
    - reference_id: PMID:26325487
      supporting_text: maturation and/or clearance of autophagic compartments under nutrient-rich conditions
    - reference_id: PMID:10660536
      supporting_text: Posttranslational geranylgeranylation of Rab24
    - reference_id: PMID:26325487
      supporting_text: targeting of RAB24 to autophagic compartments
    - reference_id: file:human/RAB24/RAB24-deep-research-falcon.md
      supporting_text: RAB24 localizes to both the inner and outer limiting membranes of autophagosomes and autophagic vacuoles
- term:
    id: GO:0003924
    label: GTPase activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: enables
  review:
    summary: GTPase activity is consistent with RAB24 being an atypical Rab-family small GTPase.
    action: ACCEPT
    reason: RAB24 is a Rab small GTPase; the evidence also cautions that it has unusually low GTP hydrolysis and is predominantly GTP-bound, but this does not negate the Rab GTPase/GTP-binding molecular-function annotation.
    supported_by:
    - reference_id: PMID:10660536
      supporting_text: Rab24 exists predominantly in the GTP state
    - reference_id: PMID:10660536
      supporting_text: The low GTPase activity is related to the presence of serine instead of glutamine
- term:
    id: GO:0003925
    label: G protein activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: enables
  review:
    summary: G protein activity is consistent with RAB24 being an atypical Rab-family small GTPase.
    action: ACCEPT
    reason: RAB24 is a Rab small GTPase; the evidence also cautions that it has unusually low GTP hydrolysis and is predominantly GTP-bound, but this does not negate the Rab GTPase/GTP-binding molecular-function annotation.
    supported_by:
    - reference_id: PMID:10660536
      supporting_text: Rab24 exists predominantly in the GTP state
    - reference_id: PMID:10660536
      supporting_text: The low GTPase activity is related to the presence of serine instead of glutamine
- term:
    id: GO:0005525
    label: GTP binding
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: enables
  review:
    summary: GTP binding is consistent with RAB24 being an atypical Rab-family small GTPase.
    action: ACCEPT
    reason: RAB24 is a Rab small GTPase; the evidence also cautions that it has unusually low GTP hydrolysis and is predominantly GTP-bound, but this does not negate the Rab GTPase/GTP-binding molecular-function annotation.
    supported_by:
    - reference_id: PMID:10660536
      supporting_text: Rab24 exists predominantly in the GTP state
    - reference_id: PMID:10660536
      supporting_text: The low GTPase activity is related to the presence of serine instead of glutamine
- term:
    id: GO:0005819
    label: spindle
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: located_in
  review:
    summary: spindle is transferred mouse oocyte/spindle biology and is not the central proteostasis function.
    action: KEEP_AS_NON_CORE
    reason: UniProt and GOA support this as by-similarity mouse-oocyte/meiosis context. It may be biologically real in a reproductive setting, but it is secondary to RAB24 basal autophagic-compartment maturation/clearance for the human PN review.
    supported_by:
    - reference_id: file:human/RAB24/RAB24-uniprot.txt
      supporting_text: Involved in the modulation of meiotic apparatus assembly and meiotic progression during oocyte maturation
    - reference_id: file:human/RAB24/RAB24-uniprot.txt
      supporting_text: possibly through regulation of kinetochore-microtubule interaction
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  qualifier: located_in
  review:
    summary: cytosol is a broad RAB24 localization/context annotation.
    action: KEEP_AS_NON_CORE
    reason: RAB24 can be cytosolic and membrane-associated, with perinuclear/autophagic-compartment localization reported by similarity, but these broad terms should not be treated as the core location when autophagosome/autophagosome membrane is available.
    supported_by:
    - reference_id: PMID:10660536
      supporting_text: Posttranslational geranylgeranylation of Rab24
    - reference_id: PMID:26325487
      supporting_text: targeting of RAB24 to autophagic compartments
    - reference_id: file:human/RAB24/RAB24-uniprot.txt
      supporting_text: Only about 20% is recovered in the particulate fraction
- term:
    id: GO:0016020
    label: membrane
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  qualifier: located_in
  review:
    summary: membrane is a broad RAB24 localization/context annotation.
    action: KEEP_AS_NON_CORE
    reason: RAB24 can be cytosolic and membrane-associated, with perinuclear/autophagic-compartment localization reported by similarity, but these broad terms should not be treated as the core location when autophagosome/autophagosome membrane is available.
    supported_by:
    - reference_id: PMID:10660536
      supporting_text: Posttranslational geranylgeranylation of Rab24
    - reference_id: PMID:26325487
      supporting_text: targeting of RAB24 to autophagic compartments
    - reference_id: file:human/RAB24/RAB24-uniprot.txt
      supporting_text: Only about 20% is recovered in the particulate fraction
- term:
    id: GO:0048471
    label: perinuclear region of cytoplasm
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: located_in
  review:
    summary: perinuclear region of cytoplasm is a broad RAB24 localization/context annotation.
    action: KEEP_AS_NON_CORE
    reason: RAB24 can be cytosolic and membrane-associated, with perinuclear/autophagic-compartment localization reported by similarity, but these broad terms should not be treated as the core location when autophagosome/autophagosome membrane is available.
    supported_by:
    - reference_id: PMID:10660536
      supporting_text: Posttranslational geranylgeranylation of Rab24
    - reference_id: PMID:26325487
      supporting_text: targeting of RAB24 to autophagic compartments
    - reference_id: file:human/RAB24/RAB24-uniprot.txt
      supporting_text: Only about 20% is recovered in the particulate fraction
- term:
    id: GO:0098588
    label: bounding membrane of organelle
  evidence_type: IEA
  original_reference_id: GO_REF:0000117
  qualifier: located_in
  review:
    summary: bounding membrane of organelle is a broad RAB24 localization/context annotation.
    action: KEEP_AS_NON_CORE
    reason: RAB24 can be cytosolic and membrane-associated, with perinuclear/autophagic-compartment localization reported by similarity, but these broad terms should not be treated as the core location when autophagosome/autophagosome membrane is available.
    supported_by:
    - reference_id: PMID:10660536
      supporting_text: Posttranslational geranylgeranylation of Rab24
    - reference_id: PMID:26325487
      supporting_text: targeting of RAB24 to autophagic compartments
    - reference_id: file:human/RAB24/RAB24-uniprot.txt
      supporting_text: Only about 20% is recovered in the particulate fraction
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:20562859
  qualifier: enables
  review:
    summary: Generic protein binding does not describe the actual RAB24 molecular function.
    action: MARK_AS_OVER_ANNOTATED
    reason: The interaction record may identify a binding partner, but protein binding is uninformative as a GO molecular function. RAB24 should be represented by Rab-family GTPase/GTP-binding activity and, where evidence is specific, autophagic-compartment localization/process terms.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:32296183
  qualifier: enables
  review:
    summary: Generic protein binding does not describe the actual RAB24 molecular function.
    action: MARK_AS_OVER_ANNOTATED
    reason: The interaction record may identify a binding partner, but protein binding is uninformative as a GO molecular function. RAB24 should be represented by Rab-family GTPase/GTP-binding activity and, where evidence is specific, autophagic-compartment localization/process terms.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:33961781
  qualifier: enables
  review:
    summary: Generic protein binding does not describe the actual RAB24 molecular function.
    action: MARK_AS_OVER_ANNOTATED
    reason: The interaction record may identify a binding partner, but protein binding is uninformative as a GO molecular function. RAB24 should be represented by Rab-family GTPase/GTP-binding activity and, where evidence is specific, autophagic-compartment localization/process terms.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:35271311
  qualifier: enables
  review:
    summary: Generic protein binding does not describe the actual RAB24 molecular function.
    action: MARK_AS_OVER_ANNOTATED
    reason: The interaction record may identify a binding partner, but protein binding is uninformative as a GO molecular function. RAB24 should be represented by Rab-family GTPase/GTP-binding activity and, where evidence is specific, autophagic-compartment localization/process terms.
- term:
    id: GO:0001556
    label: oocyte maturation
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  qualifier: involved_in
  review:
    summary: oocyte maturation is transferred mouse oocyte/spindle biology and is not the central proteostasis function.
    action: KEEP_AS_NON_CORE
    reason: UniProt and GOA support this as by-similarity mouse-oocyte/meiosis context. It may be biologically real in a reproductive setting, but it is secondary to RAB24 basal autophagic-compartment maturation/clearance for the human PN review.
    supported_by:
    - reference_id: file:human/RAB24/RAB24-uniprot.txt
      supporting_text: Involved in the modulation of meiotic apparatus assembly and meiotic progression during oocyte maturation
    - reference_id: file:human/RAB24/RAB24-uniprot.txt
      supporting_text: possibly through regulation of kinetochore-microtubule interaction
- term:
    id: GO:0005737
    label: cytoplasm
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: located_in
  review:
    summary: cytoplasm is a broad RAB24 localization/context annotation.
    action: KEEP_AS_NON_CORE
    reason: RAB24 can be cytosolic and membrane-associated, with perinuclear/autophagic-compartment localization reported by similarity, but these broad terms should not be treated as the core location when autophagosome/autophagosome membrane is available.
    supported_by:
    - reference_id: PMID:10660536
      supporting_text: Posttranslational geranylgeranylation of Rab24
    - reference_id: PMID:26325487
      supporting_text: targeting of RAB24 to autophagic compartments
    - reference_id: file:human/RAB24/RAB24-uniprot.txt
      supporting_text: Only about 20% is recovered in the particulate fraction
- term:
    id: GO:0005776
    label: autophagosome
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  qualifier: located_in
  review:
    summary: autophagosome is a core RAB24 autophagy-associated location.
    action: ACCEPT
    reason: RAB24 localizes to autophagic vacuoles/autophagic compartments and the autophagosome membrane context is directly relevant to its basal autophagic-compartment maturation/clearance role.
    supported_by:
    - reference_id: PMID:26325487
      supporting_text: localization of RAB24 to autophagic vacuoles
    - reference_id: PMID:26325487
      supporting_text: maturation and/or clearance of autophagic compartments under nutrient-rich conditions
    - reference_id: PMID:10660536
      supporting_text: Posttranslational geranylgeranylation of Rab24
    - reference_id: PMID:26325487
      supporting_text: targeting of RAB24 to autophagic compartments
- term:
    id: GO:0006914
    label: autophagy
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  qualifier: involved_in
  review:
    summary: Generic autophagy is too broad for the RAB24-specific evidence.
    action: MODIFY
    reason: The RAB24-specific study places the function at maturation and/or clearance of late autophagic compartments under basal nutrient-rich conditions, while formation and short starvation-induced autophagy are not affected. Replace the broad autophagy term with autophagosome maturation.
    proposed_replacement_terms:
    - id: GO:0097352
      label: autophagosome maturation
    supported_by:
    - reference_id: PMID:26325487
      supporting_text: localization of RAB24 to autophagic vacuoles
    - reference_id: PMID:26325487
      supporting_text: maturation and/or clearance of autophagic compartments under nutrient-rich conditions
    - reference_id: PMID:26325487
      supporting_text: Formation of autophagosomes is shown to be unaffected by RAB24-silencing with siRNA
- term:
    id: GO:0008608
    label: attachment of spindle microtubules to kinetochore
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  qualifier: involved_in
  review:
    summary: attachment of spindle microtubules to kinetochore is transferred mouse oocyte/spindle biology and is not the central proteostasis function.
    action: KEEP_AS_NON_CORE
    reason: UniProt and GOA support this as by-similarity mouse-oocyte/meiosis context. It may be biologically real in a reproductive setting, but it is secondary to RAB24 basal autophagic-compartment maturation/clearance for the human PN review.
    supported_by:
    - reference_id: file:human/RAB24/RAB24-uniprot.txt
      supporting_text: Involved in the modulation of meiotic apparatus assembly and meiotic progression during oocyte maturation
    - reference_id: file:human/RAB24/RAB24-uniprot.txt
      supporting_text: possibly through regulation of kinetochore-microtubule interaction
- term:
    id: GO:0140013
    label: meiotic nuclear division
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  qualifier: involved_in
  review:
    summary: meiotic nuclear division is transferred mouse oocyte/spindle biology and is not the central proteostasis function.
    action: KEEP_AS_NON_CORE
    reason: UniProt and GOA support this as by-similarity mouse-oocyte/meiosis context. It may be biologically real in a reproductive setting, but it is secondary to RAB24 basal autophagic-compartment maturation/clearance for the human PN review.
    supported_by:
    - reference_id: file:human/RAB24/RAB24-uniprot.txt
      supporting_text: Involved in the modulation of meiotic apparatus assembly and meiotic progression during oocyte maturation
    - reference_id: file:human/RAB24/RAB24-uniprot.txt
      supporting_text: possibly through regulation of kinetochore-microtubule interaction
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: IDA
  original_reference_id: GO_REF:0000052
  qualifier: located_in
  review:
    summary: cytosol is a broad RAB24 localization/context annotation.
    action: KEEP_AS_NON_CORE
    reason: RAB24 can be cytosolic and membrane-associated, with perinuclear/autophagic-compartment localization reported by similarity, but these broad terms should not be treated as the core location when autophagosome/autophagosome membrane is available.
    supported_by:
    - reference_id: PMID:10660536
      supporting_text: Posttranslational geranylgeranylation of Rab24
    - reference_id: PMID:26325487
      supporting_text: targeting of RAB24 to autophagic compartments
    - reference_id: file:human/RAB24/RAB24-uniprot.txt
      supporting_text: Only about 20% is recovered in the particulate fraction
- term:
    id: GO:0003925
    label: G protein activity
  evidence_type: ISS
  original_reference_id: GO_REF:0000024
  qualifier: enables
  review:
    summary: G protein activity is consistent with RAB24 being an atypical Rab-family small GTPase.
    action: ACCEPT
    reason: RAB24 is a Rab small GTPase; the evidence also cautions that it has unusually low GTP hydrolysis and is predominantly GTP-bound, but this does not negate the Rab GTPase/GTP-binding molecular-function annotation.
    supported_by:
    - reference_id: PMID:10660536
      supporting_text: Rab24 exists predominantly in the GTP state
    - reference_id: PMID:10660536
      supporting_text: The low GTPase activity is related to the presence of serine instead of glutamine
- term:
    id: GO:0003924
    label: GTPase activity
  evidence_type: ISS
  original_reference_id: GO_REF:0000024
  qualifier: enables
  review:
    summary: GTPase activity is consistent with RAB24 being an atypical Rab-family small GTPase.
    action: ACCEPT
    reason: RAB24 is a Rab small GTPase; the evidence also cautions that it has unusually low GTP hydrolysis and is predominantly GTP-bound, but this does not negate the Rab GTPase/GTP-binding molecular-function annotation.
    supported_by:
    - reference_id: PMID:10660536
      supporting_text: Rab24 exists predominantly in the GTP state
    - reference_id: PMID:10660536
      supporting_text: The low GTPase activity is related to the presence of serine instead of glutamine
- term:
    id: GO:0016020
    label: membrane
  evidence_type: EXP
  original_reference_id: PMID:10660536
  qualifier: located_in
  review:
    summary: membrane is a broad RAB24 localization/context annotation.
    action: KEEP_AS_NON_CORE
    reason: RAB24 can be cytosolic and membrane-associated, with perinuclear/autophagic-compartment localization reported by similarity, but these broad terms should not be treated as the core location when autophagosome/autophagosome membrane is available.
    supported_by:
    - reference_id: PMID:10660536
      supporting_text: Posttranslational geranylgeranylation of Rab24
    - reference_id: PMID:26325487
      supporting_text: targeting of RAB24 to autophagic compartments
    - reference_id: file:human/RAB24/RAB24-uniprot.txt
      supporting_text: Only about 20% is recovered in the particulate fraction
- term:
    id: GO:0001556
    label: oocyte maturation
  evidence_type: ISS
  original_reference_id: GO_REF:0000024
  qualifier: involved_in
  review:
    summary: oocyte maturation is transferred mouse oocyte/spindle biology and is not the central proteostasis function.
    action: KEEP_AS_NON_CORE
    reason: UniProt and GOA support this as by-similarity mouse-oocyte/meiosis context. It may be biologically real in a reproductive setting, but it is secondary to RAB24 basal autophagic-compartment maturation/clearance for the human PN review.
    supported_by:
    - reference_id: file:human/RAB24/RAB24-uniprot.txt
      supporting_text: Involved in the modulation of meiotic apparatus assembly and meiotic progression during oocyte maturation
    - reference_id: file:human/RAB24/RAB24-uniprot.txt
      supporting_text: possibly through regulation of kinetochore-microtubule interaction
- term:
    id: GO:0008608
    label: attachment of spindle microtubules to kinetochore
  evidence_type: ISS
  original_reference_id: GO_REF:0000024
  qualifier: involved_in
  review:
    summary: attachment of spindle microtubules to kinetochore is transferred mouse oocyte/spindle biology and is not the central proteostasis function.
    action: KEEP_AS_NON_CORE
    reason: UniProt and GOA support this as by-similarity mouse-oocyte/meiosis context. It may be biologically real in a reproductive setting, but it is secondary to RAB24 basal autophagic-compartment maturation/clearance for the human PN review.
    supported_by:
    - reference_id: file:human/RAB24/RAB24-uniprot.txt
      supporting_text: Involved in the modulation of meiotic apparatus assembly and meiotic progression during oocyte maturation
    - reference_id: file:human/RAB24/RAB24-uniprot.txt
      supporting_text: possibly through regulation of kinetochore-microtubule interaction
- term:
    id: GO:0140013
    label: meiotic nuclear division
  evidence_type: ISS
  original_reference_id: GO_REF:0000024
  qualifier: involved_in
  review:
    summary: meiotic nuclear division is transferred mouse oocyte/spindle biology and is not the central proteostasis function.
    action: KEEP_AS_NON_CORE
    reason: UniProt and GOA support this as by-similarity mouse-oocyte/meiosis context. It may be biologically real in a reproductive setting, but it is secondary to RAB24 basal autophagic-compartment maturation/clearance for the human PN review.
    supported_by:
    - reference_id: file:human/RAB24/RAB24-uniprot.txt
      supporting_text: Involved in the modulation of meiotic apparatus assembly and meiotic progression during oocyte maturation
    - reference_id: file:human/RAB24/RAB24-uniprot.txt
      supporting_text: possibly through regulation of kinetochore-microtubule interaction
- term:
    id: GO:0000421
    label: autophagosome membrane
  evidence_type: ISS
  original_reference_id: GO_REF:0000024
  qualifier: located_in
  review:
    summary: autophagosome membrane is a core RAB24 autophagy-associated location.
    action: ACCEPT
    reason: RAB24 localizes to autophagic vacuoles/autophagic compartments and the autophagosome membrane context is directly relevant to its basal autophagic-compartment maturation/clearance role.
    supported_by:
    - reference_id: PMID:26325487
      supporting_text: localization of RAB24 to autophagic vacuoles
    - reference_id: PMID:26325487
      supporting_text: maturation and/or clearance of autophagic compartments under nutrient-rich conditions
    - reference_id: PMID:10660536
      supporting_text: Posttranslational geranylgeranylation of Rab24
    - reference_id: PMID:26325487
      supporting_text: targeting of RAB24 to autophagic compartments
- term:
    id: GO:0006914
    label: autophagy
  evidence_type: ISS
  original_reference_id: GO_REF:0000024
  qualifier: involved_in
  review:
    summary: Generic autophagy is too broad for the RAB24-specific evidence.
    action: MODIFY
    reason: The RAB24-specific study places the function at maturation and/or clearance of late autophagic compartments under basal nutrient-rich conditions, while formation and short starvation-induced autophagy are not affected. Replace the broad autophagy term with autophagosome maturation.
    proposed_replacement_terms:
    - id: GO:0097352
      label: autophagosome maturation
    supported_by:
    - reference_id: PMID:26325487
      supporting_text: localization of RAB24 to autophagic vacuoles
    - reference_id: PMID:26325487
      supporting_text: maturation and/or clearance of autophagic compartments under nutrient-rich conditions
    - reference_id: PMID:26325487
      supporting_text: Formation of autophagosomes is shown to be unaffected by RAB24-silencing with siRNA
- term:
    id: GO:0048471
    label: perinuclear region of cytoplasm
  evidence_type: ISS
  original_reference_id: GO_REF:0000024
  qualifier: located_in
  review:
    summary: perinuclear region of cytoplasm is a broad RAB24 localization/context annotation.
    action: KEEP_AS_NON_CORE
    reason: RAB24 can be cytosolic and membrane-associated, with perinuclear/autophagic-compartment localization reported by similarity, but these broad terms should not be treated as the core location when autophagosome/autophagosome membrane is available.
    supported_by:
    - reference_id: PMID:10660536
      supporting_text: Posttranslational geranylgeranylation of Rab24
    - reference_id: PMID:26325487
      supporting_text: targeting of RAB24 to autophagic compartments
    - reference_id: file:human/RAB24/RAB24-uniprot.txt
      supporting_text: Only about 20% is recovered in the particulate fraction
- term:
    id: GO:0005739
    label: mitochondrion
  evidence_type: HTP
  original_reference_id: PMID:34800366
  qualifier: located_in
  review:
    summary: Mitochondrion is not supported as a core RAB24 location.
    action: MARK_AS_OVER_ANNOTATED
    reason: This high-throughput proteome-derived row does not match the RAB24-specific localization/function evidence, which centers on cytosol, membrane association, and autophagic compartments.
    supported_by:
    - reference_id: file:human/RAB24/RAB24-uniprot.txt
      supporting_text: Cytoplasm, cytosol
    - reference_id: PMID:26325487
      supporting_text: localization of RAB24 to autophagic vacuoles
- term:
    id: GO:0005886
    label: plasma membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-6798743
  qualifier: located_in
  review:
    summary: plasma membrane is Reactome degranulation context, not a specific RAB24 core location.
    action: MARK_AS_OVER_ANNOTATED
    reason: The reviewed RAB24 evidence supports autophagic-compartment/autophagosome membrane localization. Reactome secretory-granule/plasma-membrane context should not be propagated as a core RAB24 cellular-component annotation.
    supported_by:
    - reference_id: PMID:26325487
      supporting_text: localization of RAB24 to autophagic vacuoles
    - reference_id: PMID:26325487
      supporting_text: maturation and/or clearance of autophagic compartments under nutrient-rich conditions
- term:
    id: GO:0030667
    label: secretory granule membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-6798743
  qualifier: located_in
  review:
    summary: secretory granule membrane is Reactome degranulation context, not a specific RAB24 core location.
    action: MARK_AS_OVER_ANNOTATED
    reason: The reviewed RAB24 evidence supports autophagic-compartment/autophagosome membrane localization. Reactome secretory-granule/plasma-membrane context should not be propagated as a core RAB24 cellular-component annotation.
    supported_by:
    - reference_id: PMID:26325487
      supporting_text: localization of RAB24 to autophagic vacuoles
    - reference_id: PMID:26325487
      supporting_text: maturation and/or clearance of autophagic compartments under nutrient-rich conditions
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:16034420
  qualifier: enables
  review:
    summary: Generic protein binding does not describe the actual RAB24 molecular function.
    action: MARK_AS_OVER_ANNOTATED
    reason: The interaction record may identify a binding partner, but protein binding is uninformative as a GO molecular function. RAB24 should be represented by Rab-family GTPase/GTP-binding activity and, where evidence is specific, autophagic-compartment localization/process terms.
    supported_by:
    - reference_id: PMID:16034420
      supporting_text: Rab GTPases interact with functionally diverse effectors
    - reference_id: PMID:16034420
      supporting_text: rabenosyn-5 can achieve highly selective recognition
references:
- id: GO_REF:0000002
  title: Gene Ontology annotation through association of InterPro records with GO terms
  findings: []
- id: GO_REF:0000024
  title: Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
  findings: []
- id: GO_REF:0000033
  title: Annotation inferences using phylogenetic trees
  findings: []
- id: GO_REF:0000044
  title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
  findings: []
- id: GO_REF:0000052
  title: Gene Ontology annotation based on curation of immunofluorescence data
  findings: []
- id: GO_REF:0000107
  title: Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
  findings: []
- id: GO_REF:0000117
  title: Electronic Gene Ontology annotations created by ARBA machine learning models
  findings: []
- id: GO_REF:0000120
  title: Combined Automated Annotation using Multiple IEA Methods
  findings: []
- id: PMID:10660536
  title: Rab24 is an atypical member of the Rab GTPase family. Deficient GTPase activity, GDP dissociation inhibitor interaction, and prenylation of Rab24 expressed in cultured cells.
  findings:
  - statement: Human Rab24 is predominantly GTP-bound, has low GTPase activity, is inefficiently prenylated, and is partly membrane-associated.
- id: PMID:16034420
  title: Structural basis of family-wide Rab GTPase recognition by rabenosyn-5.
  findings:
  - statement: Rabenosyn-5/ZFYVE20 recognizes Rab GTPases through selective Rab-effector interactions, providing context for the RAB24 interaction but not a specific GO molecular function beyond Rab GTPase activity.
- id: PMID:20562859
  title: Network organization of the human autophagy system.
  findings: []
- id: PMID:32296183
  title: A reference map of the human binary protein interactome.
  findings: []
- id: PMID:33961781
  title: Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
  findings: []
- id: PMID:34800366
  title: Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
  findings: []
- id: PMID:35271311
  title: 'OpenCell: Endogenous tagging for the cartography of human cellular organization.'
  findings: []
- id: Reactome:R-HSA-6798743
  title: Exocytosis of secretory granule membrane proteins
  findings: []
- id: file:human/RAB24/RAB24-uniprot.txt
  title: UniProtKB record for human RAB24
  findings:
  - statement: UniProt summarizes RAB24 as an atypical Rab protein with low GTPase activity, predominant GTP-bound state, basal late-autophagic-vacuole clearance, and by-similarity oocyte meiotic apparatus context.
- id: file:human/RAB24/RAB24-notes.md
  title: RAB24 review notes
  findings:
  - statement: Manual PN-focused curation notes for RAB24; PN no-PMID rows were treated as context only.
- id: PMID:26325487
  title: RAB24 facilitates clearance of autophagic compartments during basal conditions.
  findings:
  - statement: RAB24 localizes to autophagic vacuoles/autophagic compartments and supports maturation/clearance of late basal autophagic compartments without affecting autophagosome formation.
- id: file:human/RAB24/RAB24-deep-research-falcon.md
  title: Falcon deep research report for RAB24
  findings:
  - statement: LLM-synthesized literature report agreeing that RAB24 is an atypical Rab with low intrinsic GTPase activity, predominantly GTP-bound, prenylation-dependent membrane targeting, and a late-stage basal-autophagy clearance role; it additionally surfaces the Rab7/RILP late-endosomal degradation interaction (Amaya 2016) and immuno-EM localization to both inner and outer autophagic-vacuole membranes.
  reference_review:
    relevance: MEDIUM
    correctness: UNVERIFIED
    review_notes: >-
      LLM synthesis of secondary reviews; not independently verified against the primary papers, which
      are not all in the publications cache (e.g. Amaya 2016 Traffic, Ylä-Anttila 2018 Small GTPases).
      The report's RAB24-specific points (low GTPase activity, predominant GTP-bound state,
      prenylation-dependent targeting, late-stage basal-autophagic-compartment clearance, Rab7/RILP
      interaction, inner/outer autophagic-vacuole membranes) are consistent with the curated UniProt
      and PMID:26325487 / PMID:10660536 evidence. However, the report repeatedly imposes the canonical
      Rab GEF/GAP/GDI/effector cycle and a definitive autophagosome-lysosome "fusion" step onto RAB24
      despite its atypical, GTP-locked, poorly-hydrolysing, partly-non-prenylated biochemistry; those
      canonical-mechanism generalizations are not anchored to RAB24-specific data and were not adopted.
core_functions:
- molecular_function:
    id: GO:0003924
    label: GTPase activity
  description: RAB24 is an atypical Rab-family small GTPase whose GTP-bound state supports targeting to autophagic compartments and late basal autophagic-compartment maturation/clearance.
  directly_involved_in:
  - id: GO:0097352
    label: autophagosome maturation
  locations:
  - id: GO:0000421
    label: autophagosome membrane
  - id: GO:0005776
    label: autophagosome
  supported_by:
  - reference_id: PMID:10660536
    supporting_text: Rab24 exists predominantly in the GTP state
  - reference_id: PMID:10660536
    supporting_text: The low GTPase activity is related to the presence of serine instead of glutamine
  - reference_id: PMID:26325487
    supporting_text: localization of RAB24 to autophagic vacuoles
  - reference_id: PMID:26325487
    supporting_text: maturation and/or clearance of autophagic compartments under nutrient-rich conditions
  - reference_id: file:human/RAB24/RAB24-uniprot.txt
    supporting_text: RAB24 is required for the clearance of late autophagic vacuoles under basal conditions
  - reference_id: file:human/RAB24/RAB24-uniprot.txt
    supporting_text: It is not needed for starvation-induced autophagy
- molecular_function:
    id: GO:0005525
    label: GTP binding
  description: RAB24 nucleotide binding is required for its autophagic-compartment targeting, but the protein is atypical because it has weak GTP hydrolysis and remains predominantly GTP-bound.
  directly_involved_in:
  - id: GO:0097352
    label: autophagosome maturation
  locations:
  - id: GO:0000421
    label: autophagosome membrane
  supported_by:
  - reference_id: PMID:10660536
    supporting_text: Rab24 exists predominantly in the GTP state
  - reference_id: PMID:10660536
    supporting_text: The low GTPase activity is related to the presence of serine instead of glutamine
  - reference_id: PMID:26325487
    supporting_text: guanine nucleotide binding are necessary for the targeting of RAB24 to autophagic compartments
proposed_new_terms: []
suggested_questions:
- question: Should RAB24 be curated directly to GO:0097352 autophagosome maturation rather than the current broad GO:0006914 autophagy rows?
  experts:
  - GO autophagy editors
  - Rab trafficking experts
- question: Is there enough human-specific evidence to retain oocyte/meiosis/spindle annotations for RAB24 outside mouse by-similarity transfer?
  experts:
  - GO reproductive biology editors
  - UniProt curators
suggested_experiments:
- description: Measure basal autophagic flux and late autophagic-compartment clearance in human RAB24 knockout/rescue cells using wild-type, nucleotide-binding-defective, and prenylation-defective RAB24 variants.
  hypothesis: RAB24 nucleotide binding and membrane targeting are required for late basal autophagic-compartment maturation/clearance.
- description: Test whether endogenous human RAB24 is required for autophagosome-lysosome fusion, autolysosome acidification, or post-fusion cargo degradation using LC3/p62 flux reporters and lysosomal inhibitors.
  hypothesis: RAB24 acts late in basal autophagy after autophagosome formation rather than during autophagy induction.

RAB24

Gene Description

Existing Annotations Review

Core Functions

RAB24 is an atypical Rab-family small GTPase whose GTP-bound state supports targeting to autophagic compartments and late basal autophagic-compartment maturation/clearance.

RAB24 nucleotide binding is required for its autophagic-compartment targeting, but the protein is atypical because it has weak GTP hydrolysis and remains predominantly GTP-bound.

References

Suggested Questions for Experts

Suggested Experiments

Deep Research

Falcon

Comprehensive Research Report: RAB24 (UniProt Q969Q5) - Functional Annotation

Gene Identity Verification

Primary Protein Function and Enzymatic Activity

GTPase Activity and Catalytic Mechanism

Substrate Specificity

Subcellular Localization

Endoplasmic Reticulum and Golgi Apparatus

Late Endosomes

Autophagic Compartments

Membrane Targeting Mechanism

Primary Biological Functions

Autophagy Regulation

Endosomal Trafficking and Degradation

Vesicular Trafficking

Signaling and Biochemical Pathways

The Autophagic Pathway

The Endocytic/Endosomal Pathway

Regulation of RAB24 Activity

Tissue-Specific Expression and Distribution

Disease Associations and Clinical Relevance

Neurodegeneration and Ataxia

Cancer

Non-Alcoholic Fatty Liver Disease (NAFLD)

Bacterial Infections

Summary Table

Recent Research Developments (2023-2024)

Conclusions

Artifacts

Citations

📚 Additional Documentation

Notes

RAB24 notes

Description cleanup note

Pn Notes

RAB24 PN Consistency Notes

Source Files Checked

Deep Research Files

AIGR Review Snapshot

PN Consistency Summary

Full Consistency Review

PN Dossier Context

PN row 1: Autophagy-Lysosome Pathway | Autophagosome closure maturation and lysosome fusion | Specific function in autophagosome maturation and lysosome fusion unknown

Note

📄 View Raw YAML