sta-1

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0000978 RNA polymerase II cis-regulatory region sequence-specific DNA binding	IBA GO_REF:0000033	ACCEPT	Summary: PAINT transfer (PTN000210448) of RNA polymerase II cis-regulatory region sequence-specific DNA binding. STA-1 recognises a conserved STAT cis element (PMID:16873887) and GFP::STA-1 ChIP-seq shows binding about 200 bp upstream of the TSS of about 20% of genes (PMID:28874466). Reason: Consistent with direct experimental evidence: STA-1 is a promoter-proximal, sequence-specific DNA-binding STAT. The node is a sound, deep STAT-family DNA-binding inference and STA-1 retains the DNA-binding domain residues needed for its function (PMID:42427644). Supporting Evidence: PMID:28874466 STA-1 was enriched close to transcription start sites (TSS) of about 20% of all genes, with an enriched binding peak located ~200 bp upstream of their TSS PMID:16873887 recognizing a cis DNA element conserved through phylogeny PMID:24058748 although many other STAT proteins, including STA-1, score positive in this assay
GO:0000981 DNA-binding transcription factor activity, RNA polymerase II-specific	IBA GO_REF:0000033	ACCEPT	Summary: PAINT transfer (PTN000210448) of DNA-binding transcription factor activity, RNA polymerase II-specific. STA-1 is a STAT that binds promoters and regulates transcription of protein-coding genes. Reason: Correct at the family level. In C. elegans the activity is predominantly repressive (PMID:28874466), so the more specific GO:0001227 is proposed as a NEW annotation and used in core_functions; this broader IBA remains correct and is retained. Supporting Evidence: PMID:28874466 STA-1 was enriched close to transcription start sites (TSS) of about 20% of all genes, with an enriched binding peak located ~200 bp upstream of their TSS PMID:28874466 These data suggest that STA-1 largely acts as a transcriptional repressor of an antiviral gene expression program.
GO:0003677 DNA binding	IEA GO_REF:0000002	ACCEPT	Summary: InterPro2GO (IPR013801 STAT DNA-binding domain) mapping to DNA binding. Reason: STA-1 has the STAT DNA-binding domain and binds DNA in vivo (ChIP-seq) and a conserved STAT element (PMID:16873887). Broad but correct. Supporting Evidence: PMID:16873887 recognizing a cis DNA element conserved through phylogeny PMID:28874466 STA-1 was enriched close to transcription start sites (TSS) of about 20% of all genes, with an enriched binding peak located ~200 bp upstream of their TSS PMID:24058748 A similar search with STA-1 produced three domains, SH2 (E-value 7.2e-31), DNA binding (E-value 1.9e-60) and STAT coiled-coil domain (E-value 8.8e-38)
GO:0003700 DNA-binding transcription factor activity	IEA GO_REF:0000002	ACCEPT	Summary: InterPro2GO (STAT, p53-like DNA-binding superfamily) mapping to DNA-binding transcription factor activity. Reason: Correct general term for a STAT transcription factor; more specific RNA polymerase II terms are captured elsewhere. Supporting Evidence: PMID:28874466 These data suggest that STA-1 largely acts as a transcriptional repressor of an antiviral gene expression program.
GO:0005515 protein binding	IPI PMID:14704431 A map of the interactome network of the metazoan C. elegans.	REMOVE	Summary: High-throughput yeast two-hybrid interaction with F37C4.5 (O44400) from the WI5 interactome map. Reason: Generic protein binding is uninformative about STA-1 function, and the single Y2H hit with an uncharacterised protein supports no more specific molecular function. Removal does not imply the interaction is false. The functionally relevant STA-1 association reported so far is with the DRH-1 signaling domain in co-IP/MS (PMID:42427644), which is not this row. Supporting Evidence: PMID:14704431 more than 4000 interactions were identified from high-throughput, yeast two-hybrid (HT=Y2H) screens
GO:0005634 nucleus	IBA GO_REF:0000033	ACCEPT	Summary: PAINT transfer (PTN000210448) of nucleus; STA-1 is nuclear in head neurons (PMID:16401427) and in uninfected intestinal cells, where it binds chromatin (PMID:28874466, PMID:42427644). Reason: Nucleus is where STA-1 acts as a promoter-bound repressor; nuclear localisation is required for its immune-repressive function (PMID:42427644). STA-1 (WB:WBGene00013111) is itself one of the node seeds, reflecting its own experimental grounding. Supporting Evidence: PMID:16401427 the nematode STAT ortholog STA-1 accumulated in the nuclei of five head neuron pairs, three of which are amphid neurons involved in dauer formation PMID:42427644 STA-1 protein disappears from nuclei of cells infected with the natural viral pathogen, Orsay virus, but remains nuclear in uninfected cells
GO:0005634 nucleus	IDA PMID:16401427 C. elegans STAT cooperates with DAF-7/TGF-beta signaling to ...	ACCEPT	Summary: Activated STA-1 accumulates in nuclei of five head neuron pairs, three of them amphid neurons involved in dauer formation. Reason: Direct localisation evidence (abstract-level cache, consistent with later intestinal studies). Core location. Supporting Evidence: PMID:16401427 the nematode STAT ortholog STA-1 accumulated in the nuclei of five head neuron pairs, three of which are amphid neurons involved in dauer formation PMID:42427644 STA-1 protein disappears from nuclei of cells infected with the natural viral pathogen, Orsay virus, but remains nuclear in uninfected cells
GO:0005634 nucleus	IDA PMID:16873887 C. elegans STAT: evolution of a regulatory switch.	ACCEPT	Summary: Wang & Levy (2006) report that activated STA-1, including mutants lacking functional coiled-coil and DNA-binding domains, accumulates in the nucleus. Reason: Abstract states activated STA-1 proteins accumulated in the nucleus; consistent with other evidence. Accept. Supporting Evidence: PMID:16873887 mutant STA-1 proteins that lack functional coiled-coil and DNA binding domains could still be activated and accumulated in the nucleus PMID:42427644 STA-1 protein disappears from nuclei of cells infected with the natural viral pathogen, Orsay virus, but remains nuclear in uninfected cells
GO:0005634 nucleus	IEA GO_REF:0000044	ACCEPT	Summary: UniProt subcellular location mapping (SL-0191 Nucleus). Reason: Consistent with experimental data. Supporting Evidence: PMID:16401427 the nematode STAT ortholog STA-1 accumulated in the nuclei of five head neuron pairs, three of which are amphid neurons involved in dauer formation PMID:42427644 STA-1 protein disappears from nuclei of cells infected with the natural viral pathogen, Orsay virus, but remains nuclear in uninfected cells
GO:0005737 cytoplasm	IBA GO_REF:0000033	ACCEPT	Summary: PAINT transfer (PTN000210448) of cytoplasm; STA-1 is cytoplasmic as well as nuclear (UniProt, PMID:16401427) and relocalises to cytoplasmic puncta in Orsay virus-infected intestinal cells (PMID:42427644). Reason: STAT proteins shuttle between cytoplasm and nucleus; cytoplasmic STA-1 is documented, and cytoplasmic sequestration with DRH-1 appears to be how repression is relieved. Its repressive activity itself is nuclear, so nucleus is the core location. Supporting Evidence: PMID:42427644 During viral infection, STA-1 forms cytoplasmic puncta that interact with the RNA viral sensor DRH-1 file:worm/sta-1/sta-1-uniprot.txt Translocated into the nucleus in response to phosphorylation
GO:0005737 cytoplasm	IDA PMID:16401427 C. elegans STAT cooperates with DAF-7/TGF-beta signaling to ...	ACCEPT	Summary: Wang & Levy (2006) report cytoplasmic as well as nuclear STA-1 (UniProt subcellular location cites this paper). Reason: Curator IDA from a paper whose full text is not cached; consistent with UniProt and with the cytoplasmic STA-1 puncta seen during infection (PMID:42427644). Supporting Evidence: PMID:42427644 During viral infection, STA-1 forms cytoplasmic puncta that interact with the RNA viral sensor DRH-1 file:worm/sta-1/sta-1-uniprot.txt Translocated into the nucleus in response to phosphorylation
GO:0005737 cytoplasm	IEA GO_REF:0000044	ACCEPT	Summary: UniProt subcellular location mapping (SL-0086 Cytoplasm). Reason: Consistent with experimental data. Supporting Evidence: PMID:42427644 During viral infection, STA-1 forms cytoplasmic puncta that interact with the RNA viral sensor DRH-1 file:worm/sta-1/sta-1-uniprot.txt Translocated into the nucleus in response to phosphorylation
GO:0006355 regulation of DNA-templated transcription	IEA GO_REF:0000002	ACCEPT	Summary: InterPro2GO mapping to regulation of DNA-templated transcription. Reason: Broad but correct: STA-1 regulates transcription of target genes, mostly as a repressor (PMID:28874466). Supporting Evidence: PMID:28874466 These data suggest that STA-1 largely acts as a transcriptional repressor of an antiviral gene expression program.
GO:0006357 regulation of transcription by RNA polymerase II	IBA GO_REF:0000033	ACCEPT	Summary: PAINT transfer (PTN000210448) of regulation of transcription by RNA polymerase II; STA-1 (WB:WBGene00013111) is among the node seeds. Reason: Directly supported: STA-1 binds promoters of protein-coding genes and represses an antiviral gene expression program (PMID:28874466). The child term GO:0000122 is proposed as NEW to capture the repressive polarity. Supporting Evidence: PMID:28874466 These data suggest that STA-1 largely acts as a transcriptional repressor of an antiviral gene expression program. PMID:28874466 STA-1 was enriched close to transcription start sites (TSS) of about 20% of all genes, with an enriched binding peak located ~200 bp upstream of their TSS
GO:0006952 defense response	IBA GO_REF:0000033	MODIFY	Summary: PAINT transfer (PTN000927860) of defense response, seeded by activating STATs (mammalian STAT1/STAT2 etc., fly Stat92E) and worm STA-2. STA-1 is involved in antiviral defense, but as a negative regulator: sta-1 mutants are 100-fold less permissive to Orsay virus (PMID:28874466) and STA-1 overexpression increases susceptibility (PMID:42427644). Reason: STA-1 does not execute defense; it restrains the antiviral gene-expression program in uninfected cells and is removed from infected-cell nuclei to de-repress it. The essence (a STAT acting in host defense) is right but the polarity matters, so the more precise regulatory term negative regulation of defense response to virus (GO:0050687) is proposed, matching MODULE c_elegans_jak_independent_stat_signaling. Propagation Review Root cause: PROPAGATION BAD Failure modes: REGULATORY SIGN INVERSION Sources checked: PANTHER:PTN000927860 · PTN000927860 SUPPORTS SOURCE BUT NOT TARGET Node seeds are STATs that execute or activate defense (vertebrate STAT1/STAT2-type, fly Stat92E, worm STA-2). STA-1 is in the same lineage but acts with opposite sign, repressing the antiviral program (PMID:28874466), so the inherited positive defense role needs refinement to a negative regulation term. Proposed replacements: negative regulation of defense response to virus Supporting Evidence: PMID:28874466 sta-1 mutants were 100-fold less permissive to infection than wild-type animals PMID:42427644 STA-1/STAT is a negative regulator of anti-viral defense PMID:42427644 STA-1 overexpression causes increased susceptibility to viral infection, in a manner dependent on conserved residues important for DNA binding, nuclear localization and phosphorylation file:worm/sta-1/sta-1-deep-research-openscientist.md loss of STA-1 makes animals more resistant to the natural Orsay virus, revealing that STA-1 normally suppresses a constitutive defense state
GO:0007165 signal transduction	IEA GO_REF:0000002	ACCEPT	Summary: InterPro2GO mapping (STAT domains) to signal transduction. Reason: Broad but defensible: STA-1 activity depends on a conserved phosphotyrosine (Y588) and responds to upstream inputs (SID-3 genetically; DRH-1 signaling), i.e. it transduces signals to the genome, though not via JAK. Supporting Evidence: PMID:16401427 sta-1 deficiency was complemented by reconstitution with wild-type protein, but not with a tyrosine mutant PMID:28874466 The fact that sid-3 mutants show loss of sta-1 repression suggests that phosphorylation of STA-1 is required for it to exert its repressive function.
GO:0007259 cell surface receptor signaling pathway via JAK-STAT	IBA GO_REF:0000033	REMOVE	Summary: PAINT transfer (PTN000927860) of cell surface receptor signaling pathway via JAK-STAT, seeded by vertebrate STATs and fly Stat92E. C. elegans has no JAK homolog and no interferon/cytokine receptor system; STA-1 acts in a JAK-independent pathway (PMID:28874466). Reason: The term presupposes a receptor-associated JAK that phosphorylates the STAT. No such kinase exists in C. elegans; STA-1 function instead requires the ACK-family tyrosine kinase SID-3 genetically and is relieved by DRH-1 signaling in infected cells. The IBA is a lineage-inappropriate transfer (projects/IBA_REVIEW.md section 14; projects/TAXON_PATHWAY_VARIANCE.md case study 1), consistent with the REMOVE of the same IBA on the paralog sta-2. STA-1 signaling is modelled instead in MODULE c_elegans_jak_independent_stat_signaling. Liongue & Ward (2013) place the assembly of the canonical JAK-STAT pathway in the bilaterian ancestor before the protostome split, so the absence of JAK in C. elegans is a lineage-specific loss; the IBD node placement is sound for the seeds, and the fix is an IRD on the nematode branch rather than moving the node. Propagation Review Root cause: PROPAGATION BAD Failure modes: LINEAGE OR TAXON MISMATCH Sources checked: PANTHER:PTN000927860 · PTN000927860 SUPPORTS SOURCE BUT NOT TARGET STAT-family node whose GO:0007259 IBD is seeded by vertebrate STATs and fly Stat92E, all genuine JAK-STAT pathway members. STA-1 descends from it into the nematode branch, which has no JAK homolog (PMID:28874466); STA-1 acts downstream of the non-JAK tyrosine kinase SID-3 instead. The inheritance needs an IRD on the nematode branch. Supporting Evidence: PMID:24058787 These came together to form the canonical JAK-STAT signaling pathway prior to the divergence of protostomia PMID:28874466 There is no conserved homolog of the JAK kinases in C. elegans PMID:28874466 despite the absence of both interferon and JAK, the C. elegans STAT homolog STA-1
GO:0040024 dauer larval development	IGI PMID:16401427 C. elegans STAT cooperates with DAF-7/TGF-beta signaling to ...	MODIFY	Summary: IGI with daf genes (WITH WBGene00000899, WBGene00000903): sta-1 mutants show a synthetic dauer-constitutive phenotype with selected TGF-beta pathway mutations. (Wang & Levy 2006, abstract-only in cache.) Reason: The experimental finding is sound and is not second-guessed; STA-1 represses dauer formation in cooperation with DAF-1/DAF-8 signaling, so its role is regulatory and of negative polarity. The more precise child term negative regulation of dauer larval development (GO:0061067) is proposed. This is a developmental role outside STA-1 antiviral repression but is the best-characterised in vivo function in neurons. Proposed replacements: negative regulation of dauer larval development Supporting Evidence: PMID:16401427 sta-1 mutants showed a synthetic dauer phenotype with selected TGF-beta mutations PMID:16401427 These results highlight a role for activated STAT proteins in repression of dauer formation PMID:16401427 sta-1 deficiency was complemented by reconstitution with wild-type protein, but not with a tyrosine mutant
GO:0040024 dauer larval development	IGI PMID:16401427 C. elegans STAT cooperates with DAF-7/TGF-beta signaling to ...	MODIFY	Summary: IGI with a daf gene (WITH WBGene00000900): synthetic dauer phenotype of sta-1 with TGF-beta pathway mutants. (Wang & Levy 2006, abstract-only in cache.) Reason: The experimental finding is sound and is not second-guessed; STA-1 represses dauer formation in cooperation with DAF-1/DAF-8 signaling, so its role is regulatory and of negative polarity. The more precise child term negative regulation of dauer larval development (GO:0061067) is proposed. This is a developmental role outside STA-1 antiviral repression but is the best-characterised in vivo function in neurons. Proposed replacements: negative regulation of dauer larval development Supporting Evidence: PMID:16401427 sta-1 mutants showed a synthetic dauer phenotype with selected TGF-beta mutations PMID:16401427 These results highlight a role for activated STAT proteins in repression of dauer formation PMID:16401427 sta-1 deficiency was complemented by reconstitution with wild-type protein, but not with a tyrosine mutant
GO:0040024 dauer larval development	IGI PMID:16401427 C. elegans STAT cooperates with DAF-7/TGF-beta signaling to ...	MODIFY	Summary: IGI with a daf gene (WITH WBGene00000903): synthetic dauer phenotype of sta-1 with TGF-beta pathway mutants. (Wang & Levy 2006, abstract-only in cache.) Reason: The experimental finding is sound and is not second-guessed; STA-1 represses dauer formation in cooperation with DAF-1/DAF-8 signaling, so its role is regulatory and of negative polarity. The more precise child term negative regulation of dauer larval development (GO:0061067) is proposed. This is a developmental role outside STA-1 antiviral repression but is the best-characterised in vivo function in neurons. Proposed replacements: negative regulation of dauer larval development Supporting Evidence: PMID:16401427 sta-1 mutants showed a synthetic dauer phenotype with selected TGF-beta mutations PMID:16401427 These results highlight a role for activated STAT proteins in repression of dauer formation PMID:16401427 sta-1 deficiency was complemented by reconstitution with wild-type protein, but not with a tyrosine mutant
GO:0040024 dauer larval development	IGI PMID:16401427 C. elegans STAT cooperates with DAF-7/TGF-beta signaling to ...	MODIFY	Summary: IGI with a daf gene (WITH WBGene00000910): synthetic dauer phenotype of sta-1 with TGF-beta pathway mutants. (Wang & Levy 2006, abstract-only in cache.) Reason: The experimental finding is sound and is not second-guessed; STA-1 represses dauer formation in cooperation with DAF-1/DAF-8 signaling, so its role is regulatory and of negative polarity. The more precise child term negative regulation of dauer larval development (GO:0061067) is proposed. This is a developmental role outside STA-1 antiviral repression but is the best-characterised in vivo function in neurons. Proposed replacements: negative regulation of dauer larval development Supporting Evidence: PMID:16401427 sta-1 mutants showed a synthetic dauer phenotype with selected TGF-beta mutations PMID:16401427 These results highlight a role for activated STAT proteins in repression of dauer formation PMID:16401427 sta-1 deficiency was complemented by reconstitution with wild-type protein, but not with a tyrosine mutant
GO:0040024 dauer larval development	IMP PMID:16401427 C. elegans STAT cooperates with DAF-7/TGF-beta signaling to ...	MODIFY	Summary: IMP with sta-1 alleles: sta-1 deficiency enhances dauer formation in TGF-beta mutant backgrounds and is rescued by wild-type but not tyrosine-mutant STA-1. (Wang & Levy 2006, abstract-only in cache.) Reason: The experimental finding is sound and is not second-guessed; STA-1 represses dauer formation in cooperation with DAF-1/DAF-8 signaling, so its role is regulatory and of negative polarity. The more precise child term negative regulation of dauer larval development (GO:0061067) is proposed. This is a developmental role outside STA-1 antiviral repression but is the best-characterised in vivo function in neurons. Proposed replacements: negative regulation of dauer larval development Supporting Evidence: PMID:16401427 sta-1 mutants showed a synthetic dauer phenotype with selected TGF-beta mutations PMID:16401427 These results highlight a role for activated STAT proteins in repression of dauer formation PMID:16401427 sta-1 deficiency was complemented by reconstitution with wild-type protein, but not with a tyrosine mutant
GO:0042127 regulation of cell population proliferation	IBA GO_REF:0000033	MARK AS OVER ANNOTATED	Summary: PAINT transfer (PTN000927860) of regulation of cell population proliferation, seeded by vertebrate STATs, fly Stat92E and a Dictyostelium STAT. Reason: No study links STA-1 to control of cell proliferation; sta-1 null mutants are viable (PMID:16873887) and the characterised roles are antiviral repression and dauer repression. The term reflects cytokine-driven proliferation control by vertebrate STATs and is not demonstrably inherited by STA-1, though it does not presuppose a JAK, so it is flagged rather than removed. Propagation Review Root cause: UNRESOLVED Failure modes: FUNCTIONAL DIVERGENCE Sources checked: PANTHER:PTN000927860 · PTN000927860 SUPPORTS SOURCE BUT NOT TARGET Seeds are vertebrate, fly and Dictyostelium STATs with proliferation phenotypes. No proliferation phenotype or target is reported for STA-1, whose characterised roles are antiviral and dauer repression; whether the nematode branch retained this role is untested. Supporting Evidence: PMID:16873887 STA-1 is not required for nematode viability, despite its widespread expression in multiple tissues of the worm
GO:0043565 sequence-specific DNA binding	IDA PMID:16873887 C. elegans STAT: evolution of a regulatory switch.	ACCEPT	Summary: Wang & Levy (2006) show STA-1 recognises a STAT cis DNA element conserved through phylogeny. Reason: Direct experimental evidence for sequence-specific DNA binding; corroborated by ChIP-seq and by the requirement of DNA-binding residues for function (PMID:28874466, PMID:42427644). Wang & Levy (2012) also report that STA-1 scores positive in an EMSA with a STAT consensus motif. Supporting Evidence: PMID:16873887 recognizing a cis DNA element conserved through phylogeny PMID:42427644 STA-1 overexpression causes increased susceptibility to viral infection, in a manner dependent on conserved residues important for DNA binding, nuclear localization and phosphorylation PMID:24058748 although many other STAT proteins, including STA-1, score positive in this assay
GO:0045944 positive regulation of transcription by RNA polymerase II	IDA PMID:16873887 C. elegans STAT: evolution of a regulatory switch.	KEEP AS NON CORE	Summary: Wang & Levy (2006) describe STA-1 as functionally related to other STATs; the IDA presumably reflects transcriptional activation in a reporter-type assay (full text not cached). Reason: Curator IDA from a paper whose full text we cannot see, so not removed. In vivo, STA-1 acts mostly as a repressor, but ChIP-seq also finds STA-1 at promoters of some genes downregulated in sta-1 mutants, so activation at a minority of targets is plausible. Retained as non-core; repression is the core activity. Supporting Evidence: PMID:28874466 Thus, although STA-1 largely acts as a constitutive repressor of gene expression, it may have a more complex role at the promoters of some genes. PMID:28874466 STA-1 binding was also enriched at the promoters of the smaller number of genes downregulated in the mutant (11/46 downregulated genes versus 122/379 upregulated genes)
GO:0001227 DNA-binding transcription repressor activity, RNA polymerase II-specific	IDA PMID:28874466 An Alternative STAT Signaling Pathway Acts in Viral Immunity...	NEW	Summary: GFP::STA-1 ChIP-seq places STA-1 ~200 bp upstream of the TSS of about 20% of genes, and genes upregulated in sta-1 null mutants are enriched for STA-1 binding; STA-1 acts mostly as a constitutive transcriptional repressor (PMID:28874466). Repression requires DNA-binding residues, nuclear localisation and Y588 (PMID:42427644). Reason: STA-1 itself binds the regulated promoters and its loss derepresses them, so it performs the repressive step (passes the participation test). This captures the repressive polarity that the broader GO:0000981 IBA does not, and supports the STA-1 annoton in MODULE c_elegans_jak_independent_stat_signaling. Supporting Evidence: PMID:28874466 These data suggest that STA-1 largely acts as a transcriptional repressor of an antiviral gene expression program. PMID:28874466 STA-1 was enriched close to transcription start sites (TSS) of about 20% of all genes, with an enriched binding peak located ~200 bp upstream of their TSS PMID:28874466 Moreover, genes upregulated in sid-3 mutants, including those shared with sta-1, were enriched for STA-1 binding by ChIP-seq PMID:42427644 STA-1 overexpression causes increased susceptibility to viral infection, in a manner dependent on conserved residues important for DNA binding, nuclear localization and phosphorylation
GO:0000122 negative regulation of transcription by RNA polymerase II	IDA PMID:28874466 An Alternative STAT Signaling Pathway Acts in Viral Immunity...	NEW	Summary: STA-1 binds promoters and represses an antiviral/anti-pathogen gene expression program in uninfected animals (PMID:28874466, PMID:42427644). Reason: STA-1 is the promoter-bound repressor, so it does the work of the process rather than being merely required for it. Child of the accepted GO:0006357 IBA, capturing polarity. Supporting Evidence: PMID:28874466 These data suggest that STA-1 largely acts as a transcriptional repressor of an antiviral gene expression program. PMID:28874466 STA-1 acts at the promoter of virus response genes and represses their expression.

Gene Description

Existing Annotations Review

Core Functions

Promoter-bound STAT transcriptional repressor that keeps an antiviral/anti-pathogen gene program repressed in uninfected intestinal cells; repression is relieved when infection removes STA-1 from the nucleus. Acts without JAK; requires Y588 and, genetically, SID-3.

Activated (tyrosine-dependent) STA-1 acts in the nuclei of head/amphid neurons to repress dauer formation in cooperation with DAF-1/DAF-8 TGF-beta signaling; its direct neuronal target genes are not known.

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