AKTIP

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0005634 nucleus	IBA GO_REF:0000033	ACCEPT	Summary: AKTIP localizes to the nucleus with enrichment at the nuclear rim in interphase, showing partial colocalization with lamins. In S phase, it transiently associates with telomeres (5-25% colocalization with TRF1 in asynchronous cells) (file:human/AKTIP/AKTIP-deep-research-falcon.md). Reason: Nuclear localization is well-supported by multiple primary studies demonstrating nuclear rim enrichment, lamin interactions, and telomeric associations. The IBA annotation is consistent with the literature. Supporting Evidence: file:human/AKTIP/AKTIP-deep-research-falcon.md Interphase: nuclear rim enrichment in puncta; intranuclear foci partially overlapping lamins; detergent-resistant nuclear signals
GO:0061631 ubiquitin conjugating enzyme activity	IBA GO_REF:0000033	REMOVE	Summary: AKTIP lacks the catalytic cysteine required for the E2 thioester-transfer reaction. Reason: The live GO:0061631 definition requires thioester-linked ubiquitin transfer involving cysteine sulfhydryl groups. PMID:26110528 identifies loss of the E2 catalytic cysteine, and PMID:18799622 characterizes FTS as an inactive E2 variant. The verified tree places AKTIP leaf PTN002545715 beneath the catalytic IBD PTN002514495. Thus target-specific catalytic-apparatus divergence, rather than an erroneous outside-clade claim, contradicts this intrinsic activity. It does not refute participation through a noncatalytic complex. Propagation Review Root cause: PROPAGATION BAD Failure modes: PSEUDO OR SUBACTIVITY LOSS Sources checked: PANTHER:PTN002514495 · PTN002514495 SUPPORTS SOURCE BUT NOT TARGET Live PANTHER v19 PTHR24068 tree connects root PTN002514495 to Q9H8T0 leaf PTN002545715. Newer local PAINT uses family PTHR24067 for the same persistent node. Target catalytic-cysteine replacement refutes this reaction; the NOT at PTN000630367 is not on the target path. See AKTIP-paint-lineage.json. Supporting Evidence: PMID:26110528 AKTIP is a UEV protein that contains a UBC domain lacking the catalytic cysteine that mediates ubiquitin transfer.
GO:0070534 protein K63-linked ubiquitination	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: Retain the inherited K63-ubiquitination process as non-core; AKTIP-specific chain-assembly machinery remains unestablished. Reason: The independently checked PAINT path places human Q9H8T0 at leaf PTN002545715 beneath IBD PTN000630262, through AKTIP subfamily node PTN004661315. The IBD includes experimentally characterized UBE2N descendants; the K63-negative IKR at PTN000630296 lies off the target path. The OpenScientist report did not reconstruct this ancestry, and its pairwise-identity/CDD and missing-interaction arguments do not demonstrate loss. Absence of the catalytic cysteine refutes intrinsic E2 chemistry but not noncatalytic process participation. PMID:36516775 Figure 3 shows altered ERalpha polyubiquitination and CAND1/CUL2 interactions after AKTIP depletion, but does not establish K63 linkage or the proposed ligase-activity mechanism. That study therefore provides context, not direct confirmation of this exact process. Retain the curated phylogenetic inference without promoting it to a proven human core mechanism. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000630262 · PTN000630262 SUPPORTS TRANSFER Confirmed positive IBD-to-target descent in live v19 PTHR24068; same PTNs occur in the newer local PTHR24067 slice. Neither K63 IKR PTN000630296 nor transferase IRD PTN000630367 is on the target path. The report supplies no target-specific loss of noncatalytic participation. Supporting Evidence: file:human/AKTIP/AKTIP-hypotheses/noncatalytic-k63-ubiquitination-and-lesion-bypass/openscientist.md Absence of interactome coverage cannot fully exclude a transient/condition-specific scaffold role. PMID:36516775 The mechanism underpinning these altered protein interactions remains to be elucidated.
GO:0006301 DNA damage tolerance	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: Retain the ancestral DNA-damage-tolerance inference as non-core while distinguishing it from demonstrated telomere-replication support. Reason: QuickGO defines GO:0006301 as bypass of single-stranded DNA lesions during replication without removing the damage. PMID:26110528 Figures 6-7 establish PCNA/RPA70 association, PCNA recruitment and TRF1-linked telomere-replication effects, not a defined lesion-bypass readout. Nevertheless, the actual positive IBD at PTN000630262 is ancestral to Q9H8T0 leaf PTN002545715, and the DNA-damage-tolerance IKR at PTN000630296 is on another branch. The report mistakes pairwise subfamily separation for exclusion from the source clade and does not establish target-specific loss. Preserve the inherited process as non-core; the human TLS/template-switch mechanism remains a follow-up question. Catalytic inactivity alone cannot exclude a structural or cofactor contribution to this BP. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000630262 · PTN000630262 SUPPORTS TRANSFER Both positive source-node placement and human target descent are verified. The source IBD includes UBE2N ortholog experiments; the report does not show that AKTIP lies outside the inferred ancestral clade. PTN000630296 IKR is not an ancestor. Human mechanistic specificity remains unestablished. Supporting Evidence: PMID:26110528 GST pull down experiments using AKTIP-GST and 293T cell extracts revealed that AKTIP precipitates both PCNA and RPA70 file:human/AKTIP/AKTIP-hypotheses/noncatalytic-k63-ubiquitination-and-lesion-bypass/openscientist.md Absence of interactome coverage cannot fully exclude a transient/condition-specific scaffold role.
GO:0005737 cytoplasm	IEA GO_REF:0000044	ACCEPT	Summary: AKTIP has cytoplasmic localization in addition to nuclear localization. It is found in the cytosol (IDA from HPA) and at the plasma membrane, and forms part of the cytoplasmic FHF complex involved in vesicle trafficking. Reason: Cytoplasmic localization is supported by multiple lines of evidence including UniProt subcellular location annotation and functional studies showing AKTIP in the FHF complex involved in cytoplasmic vesicle trafficking. Supporting Evidence: PMID:18799622 The approximately 500-kDa FHF complex contained all three Hook proteins
GO:0005886 plasma membrane	IEA GO_REF:0000044	ACCEPT	Summary: AKTIP localizes to the plasma membrane as a peripheral membrane protein, as shown in Remy & Michnick 2004 (PMID:14749367) studying AKT interaction. Reason: Plasma membrane localization is supported by experimental evidence in PMID:14749367 which showed AKTIP at the plasma membrane in context of AKT signaling. Also confirmed by IDA annotations from MGI and HPA. Supporting Evidence: PMID:14749367 The wide distribution of Ft1 in adult tissues suggests that it could be a general regulator of PKB activity
GO:0006915 apoptotic process	IEA GO_REF:0000043	KEEP AS NON CORE	Summary: AKTIP modulates the apoptotic signaling response in glucocorticoid-treated T lymphocytes. Reason: PMID:14749367 describes a PDK1/PKB/GSK3/NF-ATc cascade controlling proapoptotic Fas ligand. That mechanism supports a context-dependent apoptosis role. Later identification of FHF/ESCRT/telomere functions does not invalidate the earlier result; retain as non-core rather than over-annotated. Supporting Evidence: PMID:14749367 We demonstrate that this phenomenon occurs via a PDK1/PKB/GSK3/NF-ATc signaling cascade that controls the production of the proapoptotic hormone Fas ligand.
GO:0015031 protein transport	IEA GO_REF:0000043	ACCEPT	Summary: AKTIP is a core component of the FHF (FTS-Hook-FHIP) complex that links cytoplasmic dynein-1 to various cargos for microtubule-based transport. The FHF complex promotes vesicle trafficking via the HOPS complex and mediates perinuclear distribution of AP-4 and its cargo ATG9A. Reason: Protein transport is a genuine core function of AKTIP through its role in the FHF complex. Multiple studies demonstrate AKTIP's involvement in dynein-mediated cargo transport. Supporting Evidence: PMID:18799622 These data suggest that the FTS/Hook/FHIP complex functions to promote vesicle trafficking and/or fusion via the HOPS complex
GO:0005515 protein binding	IPI PMID:16189514 Towards a proteome-scale map of the human protein-protein in...	REMOVE	Summary: The cited interaction evidence is retained as context, but the generic protein-binding term does not specify a molecular function. Reason: PMID:16189514 reports protein interactions. Remove this uninformative GO:0005515 assertion under the annotation-reviewer policy; this does not reject the interaction or infer that the experiment assayed the wrong gene. A specific molecular function is not inferred from an interaction screen alone. Supporting Evidence: PMID:16189514 Towards a proteome-scale map of the human protein-protein interaction network.
GO:0005515 protein binding	IPI PMID:17353931 Large-scale mapping of human protein-protein interactions by...	REMOVE	Summary: The cited interaction evidence is retained as context, but the generic protein-binding term does not specify a molecular function. Reason: PMID:17353931 reports protein interactions. Remove this uninformative GO:0005515 assertion under the annotation-reviewer policy; this does not reject the interaction or infer that the experiment assayed the wrong gene. A specific molecular function is not inferred from an interaction screen alone. Supporting Evidence: PMID:17353931 Large-scale mapping of human protein-protein interactions by mass spectrometry.
GO:0005515 protein binding	IPI PMID:23414517 A human skeletal muscle interactome centered on proteins inv...	REMOVE	Summary: The cited interaction evidence is retained as context, but the generic protein-binding term does not specify a molecular function. Reason: PMID:23414517 reports protein interactions. Remove this uninformative GO:0005515 assertion under the annotation-reviewer policy; this does not reject the interaction or infer that the experiment assayed the wrong gene. A specific molecular function is not inferred from an interaction screen alone. Supporting Evidence: PMID:23414517 A human skeletal muscle interactome centered on proteins involved in muscular dystrophies: LGMD interactome.
GO:0005515 protein binding	IPI PMID:25416956 A proteome-scale map of the human interactome network.	REMOVE	Summary: The cited interaction evidence is retained as context, but the generic protein-binding term does not specify a molecular function. Reason: PMID:25416956 reports protein interactions. Remove this uninformative GO:0005515 assertion under the annotation-reviewer policy; this does not reject the interaction or infer that the experiment assayed the wrong gene. A specific molecular function is not inferred from an interaction screen alone. Supporting Evidence: PMID:25416956 A proteome-scale map of the human interactome network.
GO:0005515 protein binding	IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari...	REMOVE	Summary: The cited interaction evidence is retained as context, but the generic protein-binding term does not specify a molecular function. Reason: PMID:31515488 reports protein interactions. Remove this uninformative GO:0005515 assertion under the annotation-reviewer policy; this does not reject the interaction or infer that the experiment assayed the wrong gene. A specific molecular function is not inferred from an interaction screen alone. Supporting Evidence: PMID:31515488 Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations.
GO:0005515 protein binding	IPI PMID:32073997 The FTS-Hook-FHIP (FHF) complex interacts with AP-4 to media...	MODIFY	Summary: AKTIP is a structural component of the FHF cargo-adaptor complex. Reason: Physical FHF assembly, direct Hook association, cargo localization and reconstituted dynein transport jointly support molecular adaptor activity. This replacement specifies the established function of the interaction without assigning motor catalysis to AKTIP. Proposed replacements: molecular adaptor activity Supporting Evidence: PMID:18799622 FTS associated with a conserved C-terminal motif in Hook proteins PMID:34882091 The FTS-Hook-FHIP ('FHF') cargo adaptor complex links dynein to cargo in humans and fungi.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	REMOVE	Summary: The cited interaction evidence is retained as context, but the generic protein-binding term does not specify a molecular function. Reason: PMID:32296183 reports protein interactions. Remove this uninformative GO:0005515 assertion under the annotation-reviewer policy; this does not reject the interaction or infer that the experiment assayed the wrong gene. A specific molecular function is not inferred from an interaction screen alone. Supporting Evidence: PMID:32296183 Apr 8. A reference map of the human binary protein interactome.
GO:0005515 protein binding	IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling...	REMOVE	Summary: The cited interaction evidence is retained as context, but the generic protein-binding term does not specify a molecular function. Reason: PMID:33961781 reports protein interactions. Remove this uninformative GO:0005515 assertion under the annotation-reviewer policy; this does not reject the interaction or infer that the experiment assayed the wrong gene. A specific molecular function is not inferred from an interaction screen alone. Supporting Evidence: PMID:33961781 2021 May 6. Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
GO:0005515 protein binding	IPI PMID:34882091 Cytoplasmic dynein-1 cargo diversity is mediated by the comb...	MODIFY	Summary: AKTIP is a structural component of the FHF cargo-adaptor complex. Reason: Physical FHF assembly, direct Hook association, cargo localization and reconstituted dynein transport jointly support molecular adaptor activity. This replacement specifies the established function of the interaction without assigning motor catalysis to AKTIP. Proposed replacements: molecular adaptor activity Supporting Evidence: PMID:18799622 FTS associated with a conserved C-terminal motif in Hook proteins PMID:34882091 The FTS-Hook-FHIP ('FHF') cargo adaptor complex links dynein to cargo in humans and fungi.
GO:0005515 protein binding	IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func...	REMOVE	Summary: The cited interaction evidence is retained as context, but the generic protein-binding term does not specify a molecular function. Reason: PMID:40205054 reports protein interactions. Remove this uninformative GO:0005515 assertion under the annotation-reviewer policy; this does not reject the interaction or infer that the experiment assayed the wrong gene. A specific molecular function is not inferred from an interaction screen alone. Supporting Evidence: PMID:40205054 Apr 9. Multimodal cell maps as a foundation for structural and functional genomics.
GO:0005829 cytosol	IDA GO_REF:0000052	ACCEPT	Summary: AKTIP localizes to the cytosol based on immunofluorescence data from the Human Protein Atlas. Reason: Cytosolic localization is consistent with AKTIP's role in the cytoplasmic FHF complex for vesicle trafficking.
GO:0005886 plasma membrane	IDA GO_REF:0000052	ACCEPT	Summary: AKTIP localizes to the plasma membrane based on immunofluorescence data from HPA. Reason: Consistent with experimental data from Remy & Michnick 2004 and UniProt annotation.
GO:0098840 protein transport along microtubule	NAS PMID:34882091 Cytoplasmic dynein-1 cargo diversity is mediated by the comb...	ACCEPT	Summary: The FHF complex (containing AKTIP/FTS) links cargo to cytoplasmic dynein-1 for microtubule-based retrograde transport. AKTIP is the invariant core component of all FHF complexes identified (file:human/AKTIP/AKTIP-deep-research-falcon.md). Reason: This annotation accurately captures AKTIP's role in the FHF complex linking dynein to cargos for microtubule-based transport. Supporting Evidence: PMID:34882091 Cytoplasmic dynein-1 cargo diversity is mediated by the combinatorial assembly of FTS-Hook-FHIP complexes.
GO:0070695 FHF complex	IDA PMID:32073997 The FTS-Hook-FHIP (FHF) complex interacts with AP-4 to media...	ACCEPT	Summary: AKTIP is a core component of the FHF (FTS-Hook-FHIP) complex. This study demonstrates AKTIP interacts directly with Hook proteins (HOOK1, HOOK2, HOOK3) and FHIP proteins, forming the complex that mediates perinuclear distribution of AP-4 and ATG9A cargo. Reason: FHF complex membership is a core function of AKTIP. This is well-documented with direct experimental evidence including co-IP, mutagenesis (WF->AA disrupts interactions), and functional assays. Supporting Evidence: PMID:32073997 2020 Feb 19. The FTS-Hook-FHIP (FHF) complex interacts with AP-4 to mediate perinuclear distribution of AP-4 and its cargo ATG9A.
GO:1905719 protein localization to perinuclear region of cytoplasm	IMP PMID:32073997 The FTS-Hook-FHIP (FHF) complex interacts with AP-4 to media...	ACCEPT	Summary: AKTIP knockdown (as part of FHF complex) results in dispersal of AP-4 and ATG9A from the perinuclear region, demonstrating its role in perinuclear protein localization. Reason: This is a well-supported functional consequence of AKTIP's role in the FHF complex. The phenotype upon knockdown directly demonstrates involvement in perinuclear localization. Supporting Evidence: PMID:32073997 2020 Feb 19. The FTS-Hook-FHIP (FHF) complex interacts with AP-4 to mediate perinuclear distribution of AP-4 and its cargo ATG9A.
GO:0001934 positive regulation of protein phosphorylation	IDA PMID:14749367 Regulation of apoptosis by the Ft1 protein, a new modulator ...	KEEP AS NON CORE	Summary: Remy & Michnick 2004 reported that AKTIP enhances AKT1 phosphorylation by promoting its interaction with PDK1. This affects apoptosis susceptibility via the AKT/GSK3/NFAT cascade. Reason: While experimentally supported, this is not a core function of AKTIP. Extensive subsequent research (2015-2022) has established AKTIP's primary roles in telomere replication and ESCRT function. The AKT interaction that gave AKTIP its name represents a minor aspect of its biology. Supporting Evidence: PMID:14749367 the Ft1 protein interacts directly with PKB, enhancing the phosphorylation of both of its regulatory sites by promoting its interaction with the upstream kinase PDK1
GO:0005886 plasma membrane	IDA PMID:14749367 Regulation of apoptosis by the Ft1 protein, a new modulator ...	ACCEPT	Summary: AKTIP localizes to plasma membrane as peripheral membrane protein in context of AKT signaling. Reason: Duplicate localization annotation from same reference as IEA. Experimental support is valid. Supporting Evidence: PMID:14749367 Regulation of apoptosis by the Ft1 protein, a new modulator of protein kinase B/Akt.
GO:0032092 positive regulation of protein binding	IDA PMID:14749367 Regulation of apoptosis by the Ft1 protein, a new modulator ...	KEEP AS NON CORE	Summary: AKTIP promotes the interaction between AKT1 and PDK1, thereby enhancing AKT phosphorylation. Reason: While experimentally supported, this relates to the AKT interaction which is not AKTIP's core function. Subsequent research has established telomere and ESCRT roles as primary. Supporting Evidence: PMID:14749367 enhancing the phosphorylation of both of its regulatory sites by promoting its interaction with the upstream kinase PDK1
GO:0070695 FHF complex	IDA PMID:18799622 An FTS/Hook/p107(FHIP) complex interacts with and promotes e...	ACCEPT	Summary: Original identification of the FHF (FTS/Hook/FHIP) complex by proteomic analysis. AKTIP (FTS) identified as core component along with Hook proteins and FHIP. Reason: This is the seminal paper identifying the FHF complex. AKTIP's role as a core component is fundamental to its cellular function. Supporting Evidence: PMID:18799622 we identified a new multiprotein complex, the FHF complex, containing FTS, members of the microtubule-binding Hook family of coiled-coil proteins
GO:0005515 protein binding	IPI PMID:18799622 An FTS/Hook/p107(FHIP) complex interacts with and promotes e...	MODIFY	Summary: AKTIP is a structural component of the FHF cargo-adaptor complex. Reason: Physical FHF assembly, direct Hook association, cargo localization and reconstituted dynein transport jointly support molecular adaptor activity. This replacement specifies the established function of the interaction without assigning motor catalysis to AKTIP. Proposed replacements: molecular adaptor activity Supporting Evidence: PMID:18799622 FTS associated with a conserved C-terminal motif in Hook proteins PMID:34882091 The FTS-Hook-FHIP ('FHF') cargo adaptor complex links dynein to cargo in humans and fungi.
GO:0007032 endosome organization	IMP PMID:18799622 An FTS/Hook/p107(FHIP) complex interacts with and promotes e...	ACCEPT	Summary: AKTIP depletion affects endosomal organization through its role in the FHF complex which associates with the HOPS complex for endosome clustering. Reason: This is a core function of AKTIP through its FHF complex role. The HOPS complex interaction and effects on endosome/lysosome organization are well-documented. Supporting Evidence: PMID:18799622 the efficiency by which overexpression of the HOPS component Vps18 promotes clustering of lysosomal-associated membrane protein 1-positive endosome/lysosomes
GO:0007040 lysosome organization	IMP PMID:18799622 An FTS/Hook/p107(FHIP) complex interacts with and promotes e...	ACCEPT	Summary: AKTIP depletion affects lysosome organization through FHF/HOPS complex interaction. Reason: Part of AKTIP's core function in vesicle trafficking via FHF/HOPS complex interaction. Supporting Evidence: PMID:18799622 promotes clustering of lysosomal-associated membrane protein 1-positive endosome/lysosomes
GO:0008333 endosome to lysosome transport	IMP PMID:18799622 An FTS/Hook/p107(FHIP) complex interacts with and promotes e...	ACCEPT	Summary: AKTIP knockdown affects EGF trafficking from early endosomes to late endosomes/lysosomes. Reason: Core function of AKTIP through FHF complex. Well-supported by functional data showing trafficking defects upon AKTIP depletion. Supporting Evidence: PMID:18799622 Depletion of FTS by RNA interference affects both the trafficking of epidermal growth factor from early-to-late endosome/lysosomes
GO:0019787 ubiquitin-like protein transferase activity	NAS NOT PMID:18799622 An FTS/Hook/p107(FHIP) complex interacts with and promotes e...	ACCEPT	Summary: This is a NOT annotation explicitly stating AKTIP does NOT have ubiquitin-like protein transferase activity, consistent with it lacking the catalytic cysteine. Reason: This negative annotation is correct and important. AKTIP belongs to the inactive E2 variant family and lacks the catalytic cysteine for transferase activity. This annotation helps prevent mis-annotation based on domain homology. Supporting Evidence: PMID:18799622 Fused Toes (FTS) is a member of a small group of inactive variant E2 ubiquitin-conjugating enzyme domain-containing proteins of unknown function
GO:0030897 HOPS complex	IDA PMID:18799622 An FTS/Hook/p107(FHIP) complex interacts with and promotes e...	ACCEPT	Summary: AKTIP (via FHF complex) associates with/colocalizes with the HOPS complex (homotypic fusion and protein sorting complex) involved in endosome/lysosome trafficking. Reason: The primary study identifies FTS/AKTIP interactions with HOPS components and a functional contribution to HOPS-dependent endosome/lysosome clustering. Retain this experimentally curated association with the trafficking machinery, while identifying FHF as the specific complex in the core-function summary. Supporting Evidence: PMID:18799622 Hook proteins as well as FTS interact with members of both the class B and class C components of the homotypic vesicular protein sorting (HOPS) complex
GO:0045022 early endosome to late endosome transport	IMP PMID:18799622 An FTS/Hook/p107(FHIP) complex interacts with and promotes e...	ACCEPT	Summary: AKTIP knockdown affects trafficking from early to late endosomes, demonstrated by EGF trafficking assays. Reason: Core function through FHF/HOPS pathway. Well-documented phenotype upon AKTIP depletion. Supporting Evidence: PMID:18799622 Depletion of FTS by RNA interference affects both the trafficking of epidermal growth factor from early-to-late endosome/lysosomes
GO:0000723 telomere maintenance	IMP PMID:26110528 AKTIP/Ft1, a New Shelterin-Interacting Factor Required for T...	NEW	Summary: AKTIP supports telomere maintenance as a shelterin-associated replication factor. Reason: Direct association with shelterin and replication proteins, impaired PCNA recruitment and telomere-replication defects establish a structural contribution, beyond necessity alone. This proposal is independently supported by primary work, not inferred from a gap in other participants' annotations. No AKTIP entry was found in the cached GO-CAM index. Supporting Evidence: PMID:26110528 AKTIP physically interacts with PCNA and the RPA70 DNA replication factor. PMID:26110528 AKTIP/Ft1 works in concert with TRF1 to facilitate telomeric DNA replication.
GO:0030496 midbody	IDA PMID:34449766 AKTIP interacts with ESCRT I and is needed for the recruitme...	NEW	Summary: AKTIP localizes at the midbody and recruits ESCRT-III components during cytokinetic abscission. Reason: Primary imaging and interaction/recruitment experiments demonstrate the location and a structural contribution to cytokinesis. The proposal is based on work performed by AKTIP in the machinery, not solely depletion-induced multinucleation. No AKTIP entry was found in the cached GO-CAM index. Supporting Evidence: PMID:34449766 AKTIP interacts with the ESCRT I subunit VPS28 and forms a circular supra-structure at the midbody PMID:34449766 AKTIP is a component of the ESCRT I module and functions in the recruitment of ESCRT III components required for abscission.
GO:0000281 mitotic cytokinesis	IMP PMID:34449766 AKTIP interacts with ESCRT I and is needed for the recruitme...	NEW	Summary: AKTIP localizes at the midbody and recruits ESCRT-III components during cytokinetic abscission. Reason: Primary imaging and interaction/recruitment experiments demonstrate the location and a structural contribution to cytokinesis. The proposal is based on work performed by AKTIP in the machinery, not solely depletion-induced multinucleation. No AKTIP entry was found in the cached GO-CAM index. Supporting Evidence: PMID:34449766 AKTIP interacts with the ESCRT I subunit VPS28 and forms a circular supra-structure at the midbody PMID:34449766 AKTIP is a component of the ESCRT I module and functions in the recruitment of ESCRT III components required for abscission.

Gene Description

Existing Annotations Review

Core Functions

AKTIP is the invariant core component of FTS-Hook-FHIP (FHF) complexes that link cytoplasmic dynein-1 to various cargos for microtubule-based retrograde transport. Through FHF complex interactions with HOPS, AKTIP promotes endosome/lysosome trafficking and organization.

AKTIP functions as an ESCRT-I adaptor at the midbody during cytokinetic abscission. It binds ESCRT-I subunit VPS28 and collaborates with TSG101 to recruit ESCRT-III components (CHMP4B, IST1) for membrane scission. Forms a characteristic ring structure at the midbody dark zone.

References

Deep Research

Falcon

OpenScientist

📚 Additional Documentation

Notes

Primary Source Checks

📄 View Raw YAML