AKT-1 is one of two Caenorhabditis elegans orthologs of the AGC-family serine/threonine kinase Akt/PKB. Downstream of the DAF-2 insulin/IGF-1-like receptor and the AGE-1 PI3K, its pleckstrin homology domain binds PIP3 at the plasma membrane, where it is activated by PDK-1; it forms a kinase complex with AKT-2 and SGK-1. AKT-1 phosphorylates the FOXO transcription factor DAF-16 and the Nrf-like factor SKN-1, excluding them from the nucleus, and together with akt-2 is required to prevent constitutive dauer arrest. It also promotes cell survival, inhibiting CEP-1/p53-dependent germline apoptosis after DNA damage and embryonic apoptosis, drives germ cell proliferation via phosphorylation of the checkpoint protein MDF-1, and phosphorylates the TRPV channel OSM-9 in ASH neurons. AKT-1 activity is restrained by the PP2A regulatory subunit PPTR-1. It is expressed in neurons and other tissues remodelled during dauer formation.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0004672 protein kinase activity | IEA GO_REF:0000002 | MODIFY | Summary: IEA protein kinase activity (InterPro). Reason: Correct but general; AKT-1 is an AGC serine/threonine kinase. Proposed replacements: protein serine/threonine kinase activity Supporting Evidence: PMID:15068796 All three kinases of this complex are able to directly phosphorylate DAF-16/FKHRL1, yet have different functions in DAF-2 signaling. |
| GO:0004674 protein serine/threonine kinase activity | IBA GO_REF:0000033 | ACCEPT | Summary: IBA protein serine/threonine kinase activity (Akt subfamily). Reason: Core activity; experimentally confirmed for AKT-1. Supporting Evidence: PMID:15068796 All three kinases of this complex are able to directly phosphorylate DAF-16/FKHRL1, yet have different functions in DAF-2 signaling. |
| GO:0004674 protein serine/threonine kinase activity | IDA PMID:15068796 C. elegans SGK-1 is the critical component in the Akt/PKB ki... | ACCEPT | Summary: IDA (Hertweck et al. 2004): AKT-1, AKT-2 and SGK-1 each directly phosphorylate DAF-16. Reason: Direct kinase assay on the key physiological substrate. Supporting Evidence: PMID:15068796 All three kinases of this complex are able to directly phosphorylate DAF-16/FKHRL1, yet have different functions in DAF-2 signaling. |
| GO:0004674 protein serine/threonine kinase activity | IDA PMID:18358814 Direct inhibition of the longevity-promoting factor SKN-1 by... | ACCEPT | Summary: IDA (Tullet et al. 2008): AKT-1 phosphorylates SKN-1. Reason: Direct kinase assay on a second physiological substrate. Supporting Evidence: PMID:18358814 The IIS kinases AKT-1, -2, and SGK-1 phosphorylate SKN-1, and reduced IIS leads to constitutive SKN-1 nuclear accumulation in the intestine and SKN-1 target gene activation. |
| GO:0004674 protein serine/threonine kinase activity | IDA PMID:27824033 Promotion of behavior and neuronal function by reactive oxyg... | ACCEPT | Summary: IDA (Li et al. 2016): AKT-1 phosphorylates the TRPV channel OSM-9 at Thr10 in vitro. Reason: Direct kinase assay. Supporting Evidence: PMID:27824033 AKT phosphorylates OSM-9, and such phosphorylation is required for H2O2-induced potentiation of sensory behavior and ASH neuron function. |
| 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:15068796 All three kinases of this complex are able to directly phosphorylate DAF-16/FKHRL1, yet have different functions in DAF-2 signaling. |
| GO:0005515 protein binding | IPI PMID:15068796 C. elegans SGK-1 is the critical component in the Akt/PKB ki... | REMOVE | Summary: IPI with DAF-16 (O16850), Hertweck et al. 2004. Reason: Generic protein binding is uninformative; DAF-16 is a phosphorylation substrate of AKT-1, already captured by the kinase activity annotation. Removal does not dispute the interaction. Supporting Evidence: PMID:15068796 All three kinases of this complex are able to directly phosphorylate DAF-16/FKHRL1, yet have different functions in DAF-2 signaling. |
| GO:0005515 protein binding | IPI PMID:15068796 C. elegans SGK-1 is the critical component in the Akt/PKB ki... | MODIFY | Summary: IPI with SGK-1 (Q2PJ68), Hertweck et al. 2004. Reason: Generic protein binding is uninformative; AKT-1, AKT-2 and SGK-1 form a kinase complex; binding to another protein kinase is the informative MF. Proposed replacements: protein kinase binding 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:0005515 protein binding | IPI PMID:15068796 C. elegans SGK-1 is the critical component in the Akt/PKB ki... | MODIFY | Summary: IPI with AKT-2 (Q9XTG7), Hertweck et al. 2004. Reason: Generic protein binding is uninformative; AKT-1 complexes with the AKT-2 kinase. Proposed replacements: protein kinase binding 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:0005515 protein binding | IPI PMID:18309291 Spindle assembly checkpoint gene mdf-1 regulates germ cell p... | REMOVE | Summary: IPI with MDF-1 (G5EFM0), Watanabe et al. 2008. Reason: Generic protein binding is uninformative; MDF-1 is an AKT-1 phosphorylation substrate, already captured by kinase activity. Supporting Evidence: PMID:18309291 A substantial amount of [Ξ³- 32 P]ATP was incorporated by GSTβ·MDF-1; in contrast, none was incorporated by GST ( Figure 4A and B ), indicating that MDF-1 was phosphorylated by AKT in vitro . |
| GO:0005515 protein binding | IPI PMID:18358814 Direct inhibition of the longevity-promoting factor SKN-1 by... | REMOVE | Summary: IPI with DAF-16 (O16850), Tullet et al. 2008. Reason: Generic protein binding is uninformative; the substrate relationship is captured by kinase activity. Supporting Evidence: PMID:18358814 The IIS kinases AKT-1, -2, and SGK-1 phosphorylate SKN-1, and reduced IIS leads to constitutive SKN-1 nuclear accumulation in the intestine and SKN-1 target gene activation. |
| GO:0005515 protein binding | IPI PMID:19249087 A PP2A regulatory subunit regulates C. elegans insulin/IGF-1... | MODIFY | Summary: IPI with PPTR-1 (O18178), a PP2A B56 regulatory subunit (Padmanabhan et al. 2009). Reason: Generic protein binding is uninformative; PPTR-1 targets PP2A to AKT-1 to dephosphorylate Thr350; the informative MF is protein phosphatase 2A binding. Proposed replacements: protein phosphatase 2A binding Supporting Evidence: PMID:19249087 Following immunoprecipitation with either anti-FLAG or anti-GFP antibody, we found that PPTR-1 specifically interacts with AKT-1 and not with MYO-3β·GFP (Figure 4A; Materials and Methods). PMID:19249087 We show that PPTR-1 functions by regulating worm AKT-1 phosphorylation at Thr 350. |
| GO:0005516 calmodulin binding | IDA PMID:17580302 Ca(2+)/calmodulin directly interacts with the pleckstrin hom... | KEEP AS NON CORE | Summary: IDA calmodulin binding (Dong et al. 2007): C. elegans AKT1 binds Ca2+/CaM. Reason: Direct binding data; physiological significance in worms untested. Non-core. Supporting Evidence: PMID:17580302 we found that both human and Caenorhabditis elegans AKT1 kinases bound to CaM in a Ca(2+)-dependent manner |
| GO:0005516 calmodulin binding | IPI PMID:17854888 Ca(2+)/Calmodulin-binding proteins from the C. elegans prote... | KEEP AS NON CORE | Summary: IPI calmodulin binding from an mRNA-display screen of the worm proteome for Ca2+/CaM binders. Reason: Screen-derived but consistent with the IDA row; non-core. Supporting Evidence: PMID:17854888 The method allowed the identification of 9 known and 47 previously uncharacterized Ca(2+)-dependent CaM-binding proteins from the adult worm proteome. |
| GO:0005524 ATP binding | IEA GO_REF:0000002 | ACCEPT | Summary: IEA ATP binding. Reason: Intrinsic to kinase mechanism; kinase-dead K222M AKT-1 fails to rescue. Supporting Evidence: PMID:25383666 Expression of wild type AKT-1 or AKT-2 rescued the increased cell death phenotype of the akt-1(tm399); akt-2(tm1075) mutant, whereas expression of AKT-1(K222M) or AKT-2(K209M) did not (Supplementary Fig. |
| GO:0005547 phosphatidylinositol-3,4,5-trisphosphate binding | IDA PMID:25383666 Caspase-activated phosphoinositide binding by CNT-1 promotes... | ACCEPT | Summary: IDA PIP3 binding (Nakagawa et al. 2014): AKT-1 binds PIP3 in vitro and its PH domain is recruited to PIP3-rich plasma membrane in daf-18 mutants. Reason: Direct lipid-binding and in vivo PH-domain data; PIP3 binding is the mechanism linking AKT-1 to AGE-1. Supporting Evidence: PMID:25383666 When this transgene was crossed into daf-18(e1375) animals that are deficient in converting PIP3 to PIP2 and thus have elevated levels of PIP3, in the plasma membrane, bright GFP signals were seen on the plasma membrane, suggesting that AKT-1-PH::GFP translocated to the plasma membrane through binding to PIP3 (Fig. PMID:25383666 6c), indicating that tCNT-1a binds PIP3 with two order of magnitude higher affinity than AKT-1. |
| GO:0005547 phosphatidylinositol-3,4,5-trisphosphate binding | IEA GO_REF:0000117 | ACCEPT | Summary: IEA PIP3 binding (ARBA). Reason: Consistent with IDA. Supporting Evidence: PMID:25383666 When this transgene was crossed into daf-18(e1375) animals that are deficient in converting PIP3 to PIP2 and thus have elevated levels of PIP3, in the plasma membrane, bright GFP signals were seen on the plasma membrane, suggesting that AKT-1-PH::GFP translocated to the plasma membrane through binding to PIP3 (Fig. |
| GO:0005886 plasma membrane | IEA GO_REF:0000117 | ACCEPT | Summary: IEA plasma membrane. Reason: AKT-1 PH domain is recruited to the plasma membrane by PIP3. Supporting Evidence: PMID:25383666 When this transgene was crossed into daf-18(e1375) animals that are deficient in converting PIP3 to PIP2 and thus have elevated levels of PIP3, in the plasma membrane, bright GFP signals were seen on the plasma membrane, suggesting that AKT-1-PH::GFP translocated to the plasma membrane through binding to PIP3 (Fig. |
| GO:0006935 chemotaxis | IGI PMID:20837997 Reversal of salt preference is directed by the insulin/PI3K ... | KEEP AS NON CORE | Summary: IGI chemotaxis (with daf-18). Reason: AKT-1 contributes as the downstream kinase of DAF-2/AGE-1 signalling in sensory neurons (genetic interaction with daf-18); cell-context-specific behavioural output, non-core. Supporting Evidence: PMID:20837997 In ASER, we have previously shown that the insulin/PI 3-kinase signaling acts for starvation-induced salt chemotaxis plasticity. |
| GO:0007635 chemosensory behavior | IGI PMID:20837997 Reversal of salt preference is directed by the insulin/PI3K ... | KEEP AS NON CORE | Summary: IGI chemosensory behavior (with daf-18). Reason: AKT-1 contributes as the downstream kinase of DAF-2/AGE-1 signalling in sensory neurons (genetic interaction with daf-18); cell-context-specific behavioural output, non-core. Supporting Evidence: PMID:20837997 In ASER, we have previously shown that the insulin/PI 3-kinase signaling acts for starvation-induced salt chemotaxis plasticity. |
| GO:0008286 insulin receptor signaling pathway | IBA GO_REF:0000033 | ACCEPT | Summary: IBA insulin receptor signaling pathway. Reason: Core process; AKT-1/2 transduce DAF-2 signals. Supporting Evidence: PMID:9716402 We show here that two C. elegans Akt/PKB homologs, akt-1 and akt-2, transduce insulin receptor-like signals that inhibit dauer arrest and that AKT-1 and AKT-2 signaling are indispensable for insulin receptor-like signaling in C. elegans. |
| GO:0008286 insulin receptor signaling pathway | IEA GO_REF:0000117 | ACCEPT | Summary: IEA insulin receptor signaling pathway. Reason: Core process. Supporting Evidence: PMID:9716402 We show here that two C. elegans Akt/PKB homologs, akt-1 and akt-2, transduce insulin receptor-like signals that inhibit dauer arrest and that AKT-1 and AKT-2 signaling are indispensable for insulin receptor-like signaling in C. elegans. |
| GO:0008286 insulin receptor signaling pathway | IMP PMID:9716402 Caenorhabditis elegans Akt/PKB transduces insulin receptor-l... | ACCEPT | Summary: IMP insulin receptor signaling pathway (Paradis & Ruvkun 1998). Reason: Foundational genetics: AKT-1/AKT-2 are indispensable for DAF-2 signalling. Supporting Evidence: PMID:9716402 We show here that two C. elegans Akt/PKB homologs, akt-1 and akt-2, transduce insulin receptor-like signals that inhibit dauer arrest and that AKT-1 and AKT-2 signaling are indispensable for insulin receptor-like signaling in C. elegans. PMID:9716402 A loss-of-function mutation in the Fork head transcription factor DAF-16 relieves the requirement for Akt/PKB signaling, which indicates that AKT-1 and AKT-2 function primarily to antagonize DAF-16. |
| GO:0008340 determination of adult lifespan | IEA GO_REF:0000117 | ACCEPT | Summary: IEA determination of adult lifespan (ARBA). Reason: AKT-1 is part of the IIS cascade that limits lifespan; though SGK-1 has the larger lifespan role, AKT-1 contributes (PMID:15068796). Supporting Evidence: PMID:10638522 An insulin-like signaling cascade consisting of proteins encoded by the genes daf-2, age-1, akt-1, akt-2, daf-16 and daf-18 regulates dauer diapause, reproduction, and longevity. |
| GO:0008340 determination of adult lifespan | IMP PMID:10638522 Mechanisms of life span determination in Caenorhabditis eleg... | ACCEPT | Summary: IMP determination of adult lifespan from a review (Vanfleteren & Braeckman 1999). Reason: The cited review summarises primary data placing akt-1 in the IIS lifespan cascade; consistent with later work. Supporting Evidence: PMID:10638522 An insulin-like signaling cascade consisting of proteins encoded by the genes daf-2, age-1, akt-1, akt-2, daf-16 and daf-18 regulates dauer diapause, reproduction, and longevity. |
| GO:0008582 regulation of synaptic assembly at neuromuscular junction | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: IEA regulation of NMJ synaptic assembly. Reason: Context-specific IIS output; 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: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 IIS output 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:0009898 cytoplasmic side of plasma membrane | IDA PMID:25383666 Caspase-activated phosphoinositide binding by CNT-1 promotes... | ACCEPT | Summary: IDA cytoplasmic side of plasma membrane: AKT-1 PH::GFP localises to the plasma membrane in high-PIP3 daf-18 embryos. Reason: Direct imaging; site of AKT-1 activation. Supporting Evidence: PMID:25383666 When this transgene was crossed into daf-18(e1375) animals that are deficient in converting PIP3 to PIP2 and thus have elevated levels of PIP3, in the plasma membrane, bright GFP signals were seen on the plasma membrane, suggesting that AKT-1-PH::GFP translocated to the plasma membrane through binding to PIP3 (Fig. |
| GO:0010468 regulation of gene expression | IDA PMID:15068796 C. elegans SGK-1 is the critical component in the Akt/PKB ki... | KEEP AS NON CORE | Summary: IDA regulation of gene expression (Hertweck et al. 2004). Reason: AKT-1 regulates gene expression indirectly by phosphorylating DAF-16 and SKN-1; the term is very general and is a consequence of kinase activity. Non-core. Supporting Evidence: PMID:15068796 All three kinases of this complex are able to directly phosphorylate DAF-16/FKHRL1, yet have different functions in DAF-2 signaling. |
| GO:0010468 regulation of gene expression | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: IEA regulation of gene expression (ARBA). Reason: As above; general and indirect. Supporting Evidence: PMID:18358814 The IIS kinases AKT-1, -2, and SGK-1 phosphorylate SKN-1, and reduced IIS leads to constitutive SKN-1 nuclear accumulation in the intestine and SKN-1 target gene activation. |
| GO:0030424 axon | IDA PMID:9716402 Caenorhabditis elegans Akt/PKB transduces insulin receptor-l... | ACCEPT | Summary: IDA axon (AKT-1::GFP, Paradis & Ruvkun 1998). Reason: akt-1 is expressed in the nervous system. Supporting Evidence: PMID:9716402 akt-1 and akt-2 are expressed in overlapping patterns in the nervous system and in tissues that are remodeled during dauer formation. |
| GO:0030425 dendrite | IDA PMID:9716402 Caenorhabditis elegans Akt/PKB transduces insulin receptor-l... | ACCEPT | Summary: IDA dendrite (AKT-1::GFP). Reason: akt-1 is expressed in the nervous system. Supporting Evidence: PMID:9716402 akt-1 and akt-2 are expressed in overlapping patterns in the nervous system and in tissues that are remodeled during dauer formation. |
| GO:0033554 cellular response to stress | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: IEA cellular response to stress (ARBA). Reason: Broad term; AKT-1 represses DAF-16/SKN-1 stress programmes and mediates H2O2-induced sensory potentiation. Non-core. Supporting Evidence: PMID:18358814 The IIS kinases AKT-1, -2, and SGK-1 phosphorylate SKN-1, and reduced IIS leads to constitutive SKN-1 nuclear accumulation in the intestine and SKN-1 target gene activation. PMID:27824033 AKT phosphorylates OSM-9, and such phosphorylation is required for H2O2-induced potentiation of sensory behavior and ASH neuron function. |
| GO:0035556 intracellular signal transduction | IBA GO_REF:0000033 | ACCEPT | Summary: IBA intracellular signal transduction. Reason: AKT-1 relays PIP3 signals to DAF-16 and other substrates. Supporting Evidence: PMID:9716402 We show here that two C. elegans Akt/PKB homologs, akt-1 and akt-2, transduce insulin receptor-like signals that inhibit dauer arrest and that AKT-1 and AKT-2 signaling are indispensable for insulin receptor-like signaling in C. elegans. |
| GO:0035556 intracellular signal transduction | IEA GO_REF:0000117 | ACCEPT | Summary: IEA intracellular signal transduction. Reason: As IBA. Supporting Evidence: PMID:9716402 We show here that two C. elegans Akt/PKB homologs, akt-1 and akt-2, transduce insulin receptor-like signals that inhibit dauer arrest and that AKT-1 and AKT-2 signaling are indispensable for insulin receptor-like signaling in C. elegans. |
| GO:0042771 intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator | IMP PMID:17276923 AKT-1 regulates DNA-damage-induced germline apoptosis in C. ... | MODIFY | Summary: IMP intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator (Quevedo et al. 2007). Reason: AKT-1 negatively regulates CEP-1/p53-dependent DNA-damage-induced germline apoptosis; akt-1 loss increases apoptosis. The relationship is negative regulation, not participation. Proposed replacements: negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Supporting Evidence: PMID:17276923 In this study, we show that akt-1 and akt-2 negatively regulate DNA-damage-induced apoptosis in the C. elegans germline. PMID:17276923 The antiapoptotic activity of akt-1 is independent of its target gene daf-16 but dependent on cep-1/p53. |
| GO:0043025 neuronal cell body | IDA PMID:9716402 Caenorhabditis elegans Akt/PKB transduces insulin receptor-l... | ACCEPT | Summary: IDA neuronal cell body (AKT-1::GFP). Reason: akt-1 is expressed in neurons. Supporting Evidence: PMID:9716402 akt-1 and akt-2 are expressed in overlapping patterns in the nervous system and in tissues that are remodeled during dauer formation. |
| GO:0043025 neuronal cell body | IEA GO_REF:0000117 | ACCEPT | Summary: IEA neuronal cell body. Reason: Consistent with IDA. Supporting Evidence: PMID:9716402 akt-1 and akt-2 are expressed in overlapping patterns in the nervous system and in tissues that are remodeled during dauer formation. |
| GO:0043066 negative regulation of apoptotic process | IBA GO_REF:0000033 | ACCEPT | Summary: IBA negative regulation of apoptotic process (Akt node PTN001219338). Reason: Conserved Akt pro-survival function confirmed in worms: AKT-1 kinase activity promotes embryonic cell survival and limits germline DNA-damage apoptosis. Supporting Evidence: PMID:25383666 Expression of wild type AKT-1 or AKT-2 rescued the increased cell death phenotype of the akt-1(tm399); akt-2(tm1075) mutant, whereas expression of AKT-1(K222M) or AKT-2(K209M) did not (Supplementary Fig. PMID:17276923 In this study, we show that akt-1 and akt-2 negatively regulate DNA-damage-induced apoptosis in the C. elegans germline. |
| GO:0043536 positive regulation of blood vessel endothelial cell migration | IBA GO_REF:0000033 | REMOVE | Summary: IBA positive regulation of blood vessel endothelial cell migration, from human AKT1/AKT3 via the Akt node. Reason: Nematodes have no vasculature or blood vessel endothelium; the term cannot apply to C. elegans AKT-1. The Akt node is sound for kinase and insulin signalling, but this vertebrate-specific process should not propagate to nematodes. Propagation Review Root cause: PROPAGATION BAD Failure modes: LINEAGE OR TAXON MISMATCH Sources checked: PANTHER:PTN001219338 Β· PTN001219338 SUPPORTS SOURCE BUT NOT TARGET Akt subfamily node seeded by human AKT1/AKT3 vascular data; valid for vertebrates, not applicable to nematodes, which lack blood vessels. Supporting Evidence: PMID:9716402 We show here that two C. elegans Akt/PKB homologs, akt-1 and akt-2, transduce insulin receptor-like signals that inhibit dauer arrest and that AKT-1 and AKT-2 signaling are indispensable for insulin receptor-like signaling in C. elegans. |
| GO:0106310 protein serine kinase activity | IEA GO_REF:0000116 | ACCEPT | Summary: IEA protein serine kinase activity. Reason: Consistent with kinase data. Supporting Evidence: PMID:15068796 All three kinases of this complex are able to directly phosphorylate DAF-16/FKHRL1, yet have different functions in DAF-2 signaling. |
| GO:1902074 response to salt | IGI PMID:20837997 Reversal of salt preference is directed by the insulin/PI3K ... | KEEP AS NON CORE | Summary: IGI response to salt (with daf-18). Reason: AKT-1 contributes as the downstream kinase of DAF-2/AGE-1 signalling in sensory neurons (genetic interaction with daf-18); cell-context-specific behavioural output, non-core. Supporting Evidence: PMID:20837997 In ASER, we have previously shown that the insulin/PI 3-kinase signaling acts for starvation-induced salt chemotaxis plasticity. |
| GO:1902911 protein kinase complex | IEA GO_REF:0000117 | ACCEPT | Summary: IEA protein kinase complex. Reason: AKT-1 forms a complex with AKT-2 and SGK-1. 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:1902911 protein kinase complex | IPI PMID:15068796 C. elegans SGK-1 is the critical component in the Akt/PKB ki... | ACCEPT | Summary: IPI protein kinase complex (Hertweck et al. 2004). Reason: Co-immunoprecipitation of AKT-1, AKT-2 and SGK-1. Supporting Evidence: PMID:15068796 SGK-1 forms a protein complex with the AKT kinases, and is activated by and strictly depends on PDK-1. |
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Download this section (compressed HTML)Q: Which AKT-1 substrates mediate its daf-16-independent, cep-1-dependent anti-apoptotic activity?
Q: Does Ca2+/calmodulin binding to the AKT-1 PH domain regulate its membrane recruitment in vivo?
Experiment: Phosphoproteomics of akt-1 null versus wild-type germlines after ionizing radiation to identify AKT-1 substrates in the CEP-1 apoptotic pathway.
Hypothesis: AKT-1 directly phosphorylates a component of the CEP-1 apoptotic pathway.
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