pdk-1

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0004672 protein kinase activity	IEA GO_REF:0000002	MODIFY	Summary: IEA protein kinase activity (InterPro kinase domain). Reason: Correct but general; PDK-1 is an AGC-family serine/threonine kinase that phosphorylates the activation loop of AKT-1/2 and SGK-1. Proposed replacements: protein serine/threonine kinase activity Supporting Evidence: PMID:10364160 The activating pdk-1 mutation is located in a conserved region of the kinase domain; the equivalent amino acid substitution in human PDK1 activates its kinase activity toward mammalian Akt/PKB. PMID:15068796 SGK-1 forms a protein complex with the AKT kinases, and is activated by and strictly depends on PDK-1.
GO:0004674 protein serine/threonine kinase activity	IBA GO_REF:0000033	ACCEPT	Summary: IBA protein serine/threonine kinase activity (PDPK1 subfamily). Reason: Core activity; consistent with experimental data. Supporting Evidence: PMID:10364160 The activating pdk-1 mutation is located in a conserved region of the kinase domain; the equivalent amino acid substitution in human PDK1 activates its kinase activity toward mammalian Akt/PKB. PMID:15068796 SGK-1 forms a protein complex with the AKT kinases, and is activated by and strictly depends on PDK-1.
GO:0004674 protein serine/threonine kinase activity	IDA PMID:11274160 Caenorhabditis elegans PIAK, a phospholipid-independent kina...	ACCEPT	Summary: IDA protein serine/threonine kinase activity (PIAK study, Li et al. 2001): the PH-less PDK-1 form phosphorylates AKT at the activation-loop Thr308. Reason: Direct kinase assay; the curator attributed PIAK to this pdk-1 locus product. Supporting Evidence: PMID:11274160 PIAK phosphorylates mammalian AKT/PKB at the activating Thr(308) residue in the presence of the phosphatidylinositol (PI) 3-kinase inhibitors as well as in the absence of growth factors.
GO:0004674 protein serine/threonine kinase activity	IEA GO_REF:0000120	ACCEPT	Summary: IEA protein serine/threonine kinase activity. Reason: Consistent with experimental data. Supporting Evidence: PMID:10364160 The activating pdk-1 mutation is located in a conserved region of the kinase domain; the equivalent amino acid substitution in human PDK1 activates its kinase activity toward mammalian Akt/PKB.
GO:0004674 protein serine/threonine kinase activity	IMP PMID:15068796 C. elegans SGK-1 is the critical component in the Akt/PKB ki...	ACCEPT	Summary: IMP protein serine/threonine kinase activity (Hertweck et al. 2004): SGK-1 activation strictly depends on PDK-1. Reason: Supports PDK-1 as the activating kinase of SGK-1 and AKT kinases in vivo. Supporting Evidence: PMID:15068796 SGK-1 forms a protein complex with the AKT kinases, and is activated by and strictly depends on PDK-1.
GO:0004676 3-phosphoinositide-dependent protein kinase activity	ISS PMID:11274160 Caenorhabditis elegans PIAK, a phospholipid-independent kina...	NEW	Summary: PDK-1 is the PDPK1-subfamily AGC kinase with a C-terminal PDK1-type PH domain; it is the kinase that relays AGE-1 PI3K (PIP3) signals to AKT-1/AKT-2 and SGK-1. Reason: PDK-1 itself performs the catalytic step (activation-loop phosphorylation of AKT and SGK-1), so this is a participation, not a necessity, claim. The canonical product carries a PDK1-type PH domain (InterPro IPR033931, Pfam PF14593, SMART SM00233, CDD PH_PDK1); the PIAK study defines the phospholipid-independent PIAK form precisely by its lack of the PH domain present in PDK-1, and genetically pdk-1 is the relay for AGE-1 PI3K signals. Comparators in the same role carry this term (Drosophila Pdk1, human PDPK1). GOA has only the parent GO:0004674 for this gene; the PH-less PIAK form is better described by that parent, which remains accepted above. Supporting Evidence: PMID:11274160 PIAK is highly homologous to C. elegans and mammalian PDK 1 with the exception that the novel kinase lacks a phospholipid binding pleckstrin homology domain. file:worm/pdk-1/pdk-1-uniprot.txt InterPro; IPR033931; PDK1-typ_PH. file:worm/pdk-1/pdk-1-uniprot.txt Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PDPK1 subfamily. PMID:10364160 Therefore, pdk-1 activity is both necessary and sufficient to propagate AGE-1 PI3K signals in the DAF-2 insulin receptor-like signaling pathway.
GO:0005524 ATP binding	IEA GO_REF:0000002	ACCEPT	Summary: IEA ATP binding (kinase domain). Reason: Intrinsic to the kinase mechanism; acceptable though uninformative alone. Supporting Evidence: PMID:10364160 The activating pdk-1 mutation is located in a conserved region of the kinase domain; the equivalent amino acid substitution in human PDK1 activates its kinase activity toward mammalian Akt/PKB.
GO:0005634 nucleus	IDA PMID:10364160 A PDK1 homolog is necessary and sufficient to transduce AGE-...	KEEP AS NON CORE	Summary: IDA nucleus from the pdk-1 cloning paper (Paradis et al. 1999). Reason: The cached record is abstract-only and does not describe the PDK-1::GFP expression analysis; deferring to the curator who read the full text (UniProt records expression in neurons, intestine and hypodermis from this paper). PDK-1 signalling acts at membranes and in the cytoplasm; a nuclear pool is not central to its function. Supporting Evidence: PMID:10364160 We show here that a loss-of-function mutation in pdk-1, the C. elegans homolog of the mammalian Akt/PKB kinase PDK1, results in constitutive arrest at the dauer stage and increased life span; these phenotypes are suppressed by a loss of function mutation in daf-16.
GO:0005737 cytoplasm	IEA GO_REF:0000044	ACCEPT	Summary: IEA cytoplasm (UniProt by similarity). Reason: PDK1 is a cytoplasmic kinase recruited to PIP3 at the membrane. Supporting Evidence: PMID:25383666 PIP3 may then recruit serine–threonine kinases PDK-1, AKT-1, AKT-2, and SGK-1 to the plasma membrane by engaging their pleckstrin homology (PH) domains21–23, as has been shown with mammalian AKT9.
GO:0007611 learning or memory	IMP PMID:16950159 The insulin/PI 3-kinase pathway regulates salt chemotaxis le...	KEEP AS NON CORE	Summary: IMP learning or memory (salt chemotaxis learning). Reason: PDK-1 contributes as the AKT-activating kinase of DAF-2/AGE-1 signalling in sensory neurons; a cell-context-specific output of the pathway, valid but non-core. Supporting Evidence: PMID:16950159 Mutants of ins-1, daf-2, age-1, pdk-1, and akt-1, which encode the homologs of insulin, insulin/IGF-I receptor, PI 3-kinase, phosphoinositide-dependent kinase, and Akt/PKB, respectively, show severe defects in salt chemotaxis learning.
GO:0008286 insulin receptor signaling pathway	IBA GO_REF:0000033	ACCEPT	Summary: IBA insulin receptor signaling pathway. Reason: PDK-1 is necessary and sufficient to propagate AGE-1 PI3K signals to AKT-1/2 in the DAF-2 pathway; core process. Supporting Evidence: PMID:10364160 Therefore, pdk-1 activity is both necessary and sufficient to propagate AGE-1 PI3K signals in the DAF-2 insulin receptor-like signaling pathway. PMID:10364160 This indicates that the major function of C. elegans PDK1 is to transduce signals from AGE-1 to AKT-1 and AKT-2.
GO:0008582 regulation of synaptic assembly at neuromuscular junction	IGI PMID:23665919 Attenuation of insulin signalling contributes to FSN-1-media...	KEEP AS NON CORE	Summary: IGI regulation of NMJ synaptic assembly (fsn-1 modifier study). Reason: Context-specific output of IIS in muscle; non-core. Supporting Evidence: PMID:23665919 The aberrant synapse morphology and synaptic transmission in fsn-1 mutants are partially and specifically rescued by reducing insulin/IGF-signalling activity in postsynaptic muscles
GO:0030424 axon	IDA PMID:10364160 A PDK1 homolog is necessary and sufficient to transduce AGE-...	ACCEPT	Summary: IDA axon (PDK-1::GFP, Paradis et al. 1999). Reason: The cached record is abstract-only and does not describe the PDK-1::GFP expression analysis; deferring to the curator who read the full text (UniProt records expression in neurons, intestine and hypodermis from this paper). Supporting Evidence: PMID:10364160 We show here that a loss-of-function mutation in pdk-1, the C. elegans homolog of the mammalian Akt/PKB kinase PDK1, results in constitutive arrest at the dauer stage and increased life span; these phenotypes are suppressed by a loss of function mutation in daf-16.
GO:0034614 cellular response to reactive oxygen species	IMP PMID:28632756 Identification of ATF-7 and the insulin signaling pathway in...	MARK AS OVER ANNOTATED	Summary: IMP cellular response to reactive oxygen species (ATF-7/mtl-1 regulator study). Reason: The study measured cadmium-inducible metallothionein (mtl-1) transcription; pdk-1 loss increased mtl-1 expression. No ROS exposure or ROS-response assay for pdk-1 is reported in the full text; ROS appears only as the rationale for studying metallothionein. Over-extrapolated. Supporting Evidence: PMID:28632756 Loss of PDK-1 activity caused an increase in mtl-1 expression both in the presence and absence of cadmium, as determined by GFP expression in pmtl-1::GFP; pdk-1(sa709) nematodes (Fig 4A and S1 Table).
GO:0035556 intracellular signal transduction	IBA GO_REF:0000033	ACCEPT	Summary: IBA intracellular signal transduction. Reason: PDK-1 relays the PIP3 signal to AKT/SGK kinases. Supporting Evidence: PMID:10364160 This indicates that the major function of C. elegans PDK1 is to transduce signals from AGE-1 to AKT-1 and AKT-2.
GO:0040024 dauer larval development	IGI PMID:10364160 A PDK1 homolog is necessary and sufficient to transduce AGE-...	ACCEPT	Summary: IGI dauer larval development (with daf-16). Reason: pdk-1 loss causes constitutive dauer arrest suppressed by daf-16. Supporting Evidence: PMID:10364160 We show here that a loss-of-function mutation in pdk-1, the C. elegans homolog of the mammalian Akt/PKB kinase PDK1, results in constitutive arrest at the dauer stage and increased life span; these phenotypes are suppressed by a loss of function mutation in daf-16.
GO:0040024 dauer larval development	IGI PMID:10364160 A PDK1 homolog is necessary and sufficient to transduce AGE-...	ACCEPT	Summary: IGI dauer larval development (with age-1). Reason: Activating pdk-1 alleles bypass age-1 for non-dauer development. Supporting Evidence: PMID:10364160 Therefore, pdk-1 activity is both necessary and sufficient to propagate AGE-1 PI3K signals in the DAF-2 insulin receptor-like signaling pathway.
GO:0040024 dauer larval development	IGI PMID:10364160 A PDK1 homolog is necessary and sufficient to transduce AGE-...	ACCEPT	Summary: IGI dauer larval development (with akt-1/akt-2). Reason: The activating pdk-1 mutation requires akt-1 and akt-2 to suppress age-1 dauer arrest. Supporting Evidence: PMID:10364160 The activating mutation in pdk-1 requires akt-1 and akt-2 gene activity in order to suppress the dauer arrest phenotype of age-1.
GO:0040024 dauer larval development	IGI PMID:10364160 A PDK1 homolog is necessary and sufficient to transduce AGE-...	ACCEPT	Summary: IGI dauer larval development (genetic interaction row). Reason: Same paper; consistent. Supporting Evidence: PMID:10364160 Therefore, pdk-1 activity is both necessary and sufficient to propagate AGE-1 PI3K signals in the DAF-2 insulin receptor-like signaling pathway.
GO:0040024 dauer larval development	IMP PMID:10364160 A PDK1 homolog is necessary and sufficient to transduce AGE-...	ACCEPT	Summary: IMP dauer larval development. Reason: pdk-1 loss-of-function causes constitutive dauer arrest. Supporting Evidence: PMID:10364160 We show here that a loss-of-function mutation in pdk-1, the C. elegans homolog of the mammalian Akt/PKB kinase PDK1, results in constitutive arrest at the dauer stage and increased life span; these phenotypes are suppressed by a loss of function mutation in daf-16.
GO:0043025 neuronal cell body	IDA PMID:10364160 A PDK1 homolog is necessary and sufficient to transduce AGE-...	ACCEPT	Summary: IDA neuronal cell body (PDK-1::GFP). Reason: The cached record is abstract-only and does not describe the PDK-1::GFP expression analysis; deferring to the curator who read the full text (UniProt records expression in neurons, intestine and hypodermis from this paper). Supporting Evidence: PMID:10364160 We show here that a loss-of-function mutation in pdk-1, the C. elegans homolog of the mammalian Akt/PKB kinase PDK1, results in constitutive arrest at the dauer stage and increased life span; these phenotypes are suppressed by a loss of function mutation in daf-16.
GO:0048638 regulation of developmental growth	IEA GO_REF:0000117	MARK AS OVER ANNOTATED	Summary: ARBA IEA regulation of developmental growth. Reason: Machine-learned term without specific evidence for PDK-1 controlling growth per se in C. elegans; developmental roles are captured by dauer terms. Supporting Evidence: PMID:10364160 We show here that a loss-of-function mutation in pdk-1, the C. elegans homolog of the mammalian Akt/PKB kinase PDK1, results in constitutive arrest at the dauer stage and increased life span; these phenotypes are suppressed by a loss of function mutation in daf-16.
GO:0050920 regulation of chemotaxis	IMP PMID:16950159 The insulin/PI 3-kinase pathway regulates salt chemotaxis le...	KEEP AS NON CORE	Summary: IMP regulation of chemotaxis (salt chemotaxis learning). Reason: PDK-1 contributes as the AKT-activating kinase of DAF-2/AGE-1 signalling in sensory neurons; a cell-context-specific output of the pathway, valid but non-core. Supporting Evidence: PMID:16950159 Mutants of ins-1, daf-2, age-1, pdk-1, and akt-1, which encode the homologs of insulin, insulin/IGF-I receptor, PI 3-kinase, phosphoinositide-dependent kinase, and Akt/PKB, respectively, show severe defects in salt chemotaxis learning.
GO:0071248 cellular response to metal ion	IMP PMID:28632756 Identification of ATF-7 and the insulin signaling pathway in...	KEEP AS NON CORE	Summary: IMP cellular response to metal ion: pdk-1 loss alters cadmium-inducible mtl-1 transcription. Reason: Valid but indirect: PDK-1 acts through AKT-1/2 to repress mtl-1 transcription; non-core. Supporting Evidence: PMID:28632756 Loss of PDK-1 activity caused an increase in mtl-1 expression both in the presence and absence of cadmium, as determined by GFP expression in pmtl-1::GFP; pdk-1(sa709) nematodes (Fig 4A and S1 Table).
GO:0106310 protein serine kinase activity	IEA GO_REF:0000116	ACCEPT	Summary: IEA protein serine kinase activity (RHEA mapping). Reason: Consistent with serine/threonine kinase activity. Supporting Evidence: PMID:10364160 The activating pdk-1 mutation is located in a conserved region of the kinase domain; the equivalent amino acid substitution in human PDK1 activates its kinase activity toward mammalian Akt/PKB.
GO:0160108 animal gross anatomical part developmental process	IEA GO_REF:0000117	MARK AS OVER ANNOTATED	Summary: ARBA IEA animal gross anatomical part developmental process. Reason: Vague machine-learned term without specific supporting evidence. Supporting Evidence: PMID:10364160 We show here that a loss-of-function mutation in pdk-1, the C. elegans homolog of the mammalian Akt/PKB kinase PDK1, results in constitutive arrest at the dauer stage and increased life span; these phenotypes are suppressed by a loss of function mutation in daf-16.
GO:1901701 cellular response to oxygen-containing compound	IEA GO_REF:0000117	MARK AS OVER ANNOTATED	Summary: ARBA IEA cellular response to oxygen-containing compound. Reason: Vague machine-learned term; not a demonstrated PDK-1 function. Supporting Evidence: PMID:28632756 Loss of PDK-1 activity caused an increase in mtl-1 expression both in the presence and absence of cadmium, as determined by GFP expression in pmtl-1::GFP; pdk-1(sa709) nematodes (Fig 4A and S1 Table).

Gene Description

Existing Annotations Review

Core Functions

3-phosphoinositide-dependent serine/threonine kinase that phosphorylates and activates AKT-1, AKT-2 and SGK-1, relaying AGE-1 PI3K signals in the DAF-2 insulin receptor-like pathway.

Prevention of dauer arrest through activation of AKT kinases that repress DAF-16.

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