BCY1

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0000785 chromatin	IEA GO_REF:0000107	REMOVE	Summary: Ensembl Compara transfer from S. cerevisiae Bcy1. The current C. albicans Bcy1 localization data support a mostly cytosolic holoenzyme plus conditional vacuolar-membrane and cytoplasmic RNP foci, not a stable chromatin pool. Reason: The chromatin localization row is an over-transfer from budding yeast. The 2025 C. albicans functional Bcy1-GFP study reports cytosolic, vacuolar-peripheral, P-body, and stress-granule pools under tested conditions, and specifically found that Bcy1 is largely excluded from the nucleus. No C. albicans chromatin activity or chromatin localization has direct support. Supporting Evidence: PMID:39998251 Bcy1 is largely excluded from the nucleus under both conditions
GO:0000932 P-body	IDA PMID:39998251 Exploring the differential localization of protein kinase A ...	KEEP AS NON CORE	Summary: Functional Bcy1-GFP colocalized with the P-body marker Dhh1-mScarlet in response to elevated temperature. Reason: The localization was directly imaged with endogenous fluorescent fusions and is retained as a conditional, stress-induced site for PKA subunits. It is not the primary compartment for Bcy1's PKA-regulatory activity, which is mainly cytosolic. Supporting Evidence: PMID:39998251 Strong association was seen between Dhh1-mSc and mNG-Tpk1, mNG-Tpk2, and Bcy1-GFP
GO:0004862 cAMP-dependent protein kinase inhibitor activity	IBA GO_REF:0000033	ACCEPT	Summary: PAINT places cAMP-dependent protein kinase inhibitor activity at the PTHR11635 root node PTN004280545. Bcy1 is the conserved regulatory subunit that keeps Candida PKA inactive until cAMP binding releases the Tpk catalytic subunits. Reason: This is a correct core molecular function for Candida Bcy1 and is corroborated by C. albicans genetics and biochemistry: a bcy1 tpk2 mutant has constitutive cAMP-independent PKA activity, Bcy1 coimmunoprecipitates with Tpk1-GFP, and BCY1 overexpression suppresses filamentation in several hyphal-induction settings. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN004280545 · PTN004280545 SUPPORTS TRANSFER PAINT places the cAMP-binding, PKA-complex, catalytic-subunit-binding, and PKA-inhibitory activities on the PTHR11635 root; Bcy1 is a fungal PKA regulatory subunit in that conserved clade. Supporting Evidence: PMID:14871949 protein kinase A activity in the bcy1 tpk2 mutant was independent of the presence of cAMP PMID:42506221 Supporting this, overexpression of Bcy1 blocked iron-induced hyphal formation
GO:0004862 cAMP-dependent protein kinase inhibitor activity	IEA GO_REF:0000107	ACCEPT	Summary: Ensembl Compara transfer from the S. cerevisiae Bcy1 ortholog. The transferred specific inhibitor-activity term matches the accepted PAINT inference and the Candida mutant phenotypes. Reason: The S. cerevisiae source is the direct ortholog and the term captures the regulatory subunit's conserved function: Bcy1 inhibits PKA catalytic subunits in the absence of cAMP and releases them when cAMP binds. Supporting Evidence: PMID:14871949 protein kinase A activity in the bcy1 tpk2 mutant was independent of the presence of cAMP
GO:0005634 nucleus	IBA GO_REF:0000033	UNDECIDED	Summary: PAINT places nuclear activity at fungal node PTN000908765, seeded by CGD, PomBase, and SGD descendants. C. albicans-specific localization evidence is internally conflicted: the 2006 Bcy1-GFP abstract supports a nuclear pool, whereas 2025 functional Bcy1-GFP imaging reports that Bcy1 is largely excluded from nuclei in glucose and glycerol. Reason: The IBA is not circular merely because the C. albicans experimental annotation seeded the PAINT node, and nuclear localization is plausible in fungal PKA regulatory subunits. However, the older Candida full text is not cached and a newer full-text endogenous-tagging study with a functional Bcy1-GFP protein contradicts persistent nuclear localization. The right resolution may be condition-specific nuclear shuttling, a tagging difference, or a true older localization artifact, so this row is left unresolved. Propagation Review Root cause: UNRESOLVED Failure modes: COMPARTMENT OR COMPLEX MISMATCH Sources checked: PANTHER:PTN000908765 · PTN000908765 UNRESOLVED Fungal node seeded by CGD, PomBase, and SGD nuclear-localization evidence; Candida-specific Bcy1-GFP data now conflict across publications. Supporting Evidence: PMID:16473139 nuclear localization of the regulatory subunit PMID:39998251 Bcy1 is largely excluded from the nucleus under both conditions
GO:0005634 nucleus	IDA PMID:16473139 Expression levels and subcellular localization of Bcy1p in C...	UNDECIDED	Summary: This abstract-only Bcy1p-GFP study reports subcellular localization consistent with the authors' nuclear-localization model. Reason: The abstract supports nuclear localization, and the CGD curator likely had the full text. A newer, full-text study of a functional endogenous Bcy1-GFP allele reports that Bcy1 is largely excluded from nuclei in glucose and glycerol. With the 2006 full text unavailable, the conflict cannot be resolved. Supporting Evidence: PMID:16473139 nuclear localization of the regulatory subunit PMID:39998251 Bcy1 is largely excluded from the nucleus under both conditions
GO:0005634 nucleus	IEA GO_REF:0000120	UNDECIDED	Summary: Automated UniProt transfer of nuclear localization, apparently from the S. cerevisiae ortholog and ARBA. The inference is plausible but currently conflicts with newer direct Candida imaging. Reason: Nuclear localization transfers across some fungi, but C. albicans Bcy1 now has contradictory organism-specific evidence. This automated row is therefore left unresolved rather than accepted as a core location. Supporting Evidence: PMID:39998251 Bcy1 is largely excluded from the nucleus under both conditions
GO:0005634 nucleus	NAS PMID:14871949 Candida albicans lacking the gene encoding the regulatory su...	REMOVE	Summary: The 2004 paper did not directly assay Bcy1 localization; it visualized Tpk1-GFP and made a non-traceable statement about preliminary Bcy1-GFP observations. Reason: This NAS row is too weak to retain as a Candida Bcy1 nuclear-localization annotation. The authors explicitly stated that Bcy1p was not visualized directly in the experiments reported in the paper and only cited preliminary laboratory observations; those preliminary data are now contradicted by a full-text functional Bcy1-GFP study in which Bcy1 was largely nucleus-excluded. Supporting Evidence: PMID:14871949 Although Bcy1p was not visualized directly in our experiments PMID:39998251 Bcy1 is largely excluded from the nucleus under both conditions
GO:0005737 cytoplasm	IEA GO_REF:0000120	MODIFY	Summary: Automated transfer to the broad cytoplasm term. Direct Candida imaging and the PAINT row support the more precise cytosol location for the main Bcy1 pool. Reason: Bcy1 is a soluble PKA regulatory subunit, and functional Bcy1-GFP imaging shows the holoenzyme is mainly cytosolic. The cytoplasm parent should be replaced by cytosol. Proposed replacements: cytosol Supporting Evidence: PMID:39998251 the PKA holoenzyme is mainly cytosolic
GO:0005774 vacuolar membrane	IDA PMID:39998251 Exploring the differential localization of protein kinase A ...	KEEP AS NON CORE	Summary: Functional Bcy1-GFP was enriched on the vacuolar membrane when cells were grown on glycerol, and this vacuolar recruitment required Tpk2. Reason: Retained as a direct but carbon-source-specific localization of a Tpk2-containing PKA holoenzyme subpopulation, not as Bcy1's constitutive or primary site of action. Supporting Evidence: PMID:39998251 Tpk2 and Bcy1 localize to the vacuolar membrane when C. albicans utilize an alternative carbon source such as glycerol
GO:0005829 cytosol	IBA GO_REF:0000033	ACCEPT	Summary: PAINT transfers cytosolic activity from PTN000180782. This agrees with direct C. albicans imaging showing a mainly cytosolic PKA holoenzyme. Reason: Cytosol is the primary compartment for the Candida Bcy1-Tpk holoenzyme and for Bcy1's regulatory-subunit function. The PAINT placement is sound. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000180782 · PTN000180782 SUPPORTS TRANSFER Node transfers cytosol to Bcy1 and other PKA regulatory subunits; direct Candida imaging independently supports the same location. Supporting Evidence: PMID:39998251 the PKA holoenzyme is mainly cytosolic
GO:0005829 cytosol	IDA PMID:39998251 Exploring the differential localization of protein kinase A ...	ACCEPT	Summary: Functional Bcy1-GFP imaging showed that the PKA holoenzyme is mainly cytosolic. Reason: This is the best direct localization for the main Bcy1 pool and matches the conserved PKA regulatory-subunit role. Supporting Evidence: PMID:39998251 the PKA holoenzyme is mainly cytosolic
GO:0005886 plasma membrane	IEA GO_REF:0000107	REMOVE	Summary: Ensembl Compara transfer of a S. cerevisiae Bcy1 plasma-membrane row. Candida Bcy1 is soluble and has direct cytosolic, vacuolar-membrane, P-body, and stress-granule evidence, but no plasma-membrane evidence. Reason: The plasma-membrane annotation is not supported for C. albicans Bcy1. The conditional membrane-associated pool directly observed in Candida is on the vacuolar membrane during growth on glycerol. Supporting Evidence: PMID:39998251 Tpk2 and Bcy1, but not Tpk1, were enriched around the vacuolar membrane
GO:0005952 cAMP-dependent protein kinase complex	IBA GO_REF:0000033	ACCEPT	Summary: PAINT places PKA complex membership at PTN004280545. Bcy1 is the regulatory subunit in the Candida PKA holoenzyme. Reason: The inferred complex-membership row is a direct expression of Bcy1's core role as the PKA regulatory subunit; C. albicans native PKA was purified as a tetramer of two regulatory and two catalytic subunits, and Bcy1-GFP is a functional component of the holoenzyme. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN004280545 · PTN004280545 SUPPORTS TRANSFER PANTHER root node for the conserved cAMP-dependent protein kinase regulatory-subunit family. Supporting Evidence: PMID:9523695 two regulatory (R) subunits of 64 kDa PMID:39998251 Bcy1-GFP was able to maintain growth comparable with cells expressing wild-type Bcy1
GO:0005952 cAMP-dependent protein kinase complex	IDA PMID:39998251 Exploring the differential localization of protein kinase A ...	ACCEPT	Summary: This row is supported by the functional Bcy1-GFP study and by native PKA purification identifying Candida PKA as a tetramer with two regulatory subunits and two catalytic subunits. Reason: Bcy1 is the regulatory subunit of the Candida cAMP-dependent protein kinase complex; functional Bcy1-GFP was used to track the PKA holoenzyme in living cells. Supporting Evidence: PMID:9523695 two regulatory (R) subunits of 64 kDa PMID:39998251 Bcy1-GFP was able to maintain growth comparable with cells expressing wild-type Bcy1
GO:0005952 cAMP-dependent protein kinase complex	IEA GO_REF:0000002	ACCEPT	Summary: InterPro2GO mapping from the PKA regulatory-subunit signatures carried by Q9HEW1. Reason: This family-level mapping is specific and matches the experimentally supported Candida PKA regulatory-subunit role. Supporting Evidence: PMID:9523695 two regulatory (R) subunits of 64 kDa
GO:0006995 cellular response to nitrogen starvation	IEA GO_REF:0000107	REMOVE	Summary: Ensembl Compara transfer from S. cerevisiae Bcy1 to a starvation response term. Candida Bcy1 regulates PKA, which is required for many nutrient and stress responses, but the specific nitrogen-starvation process has not been established. Reason: This is an over-transfer of a condition-specific budding yeast process. The Candida rows should remain on direct PKA regulation and directly assayed conditional phenotypes rather than on a nitrogen-starvation process without Candida evidence.
GO:0007189 adenylate cyclase-activating G protein-coupled receptor signaling pathway	IBA GO_REF:0000033	ACCEPT	Summary: PAINT transfers a GPCR-to-adenylate-cyclase pathway term within the PTHR11635 regulatory-chain-only family. Bcy1 is the cAMP-binding PKA regulatory subunit that couples the upstream Cyr1-generated cAMP signal to downstream Tpk release. Reason: GO:0007189 covers the signaling series downstream of an adenylate-cyclase-activating GPCR through cAMP-dependent effector activation, not only the receptor and Cyr1 step. C. albicans has an upstream Gpr1/Gpa2-to-Cyr1 branch, and Bcy1 is the cAMP-responsive regulatory subunit of the PKA holoenzyme within that pathway. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000180782 · PTN000180782 SUPPORTS TRANSFER Node transfers this cAMP-pathway BP from mammalian, S. pombe, and Dictyostelium PKA regulatory subunits; the Bcy1-family regulatory chain is an in-pathway cAMP sensor rather than a false source clade. Supporting Evidence: PMID:14871949 protein kinase A activity in the bcy1 tpk2 mutant was independent of the presence of cAMP
GO:0008603 cAMP-dependent protein kinase regulator activity	IDA PMID:9523695 Isolation and characterisation of cAMP-dependent protein kin...	ACCEPT	Summary: Native Candida PKA was purified and characterized as a cAMP-responsive tetramer with two regulatory subunits and two catalytic subunits, and 8-azido-cAMP photoaffinity labeling indicated a single native R-subunit type. Reason: Although this 1998 paper predates BCY1 cloning, C. albicans encodes a single PKA regulatory subunit and the purified native R subunit is Bcy1. The broad regulator-activity term is accurate and is refined by the accepted PKA inhibitor activity row. Supporting Evidence: PMID:9523695 two regulatory (R) subunits of 64 kDa PMID:9523695 Photoaffinity labeling with 8-azido-[32P]cAMP of crude extracts from yeast and mycelial cells strongly suggests that only one type of R subunit is present in the fungus
GO:0008603 cAMP-dependent protein kinase regulator activity	IEA GO_REF:0000120	MODIFY	Summary: Automated mapping from PKA regulatory-subunit signatures to a correct but general molecular function. Reason: The PKA regulatory-subunit family annotation is sound, but Candida Bcy1's specific role is to inhibit PKA catalytic subunits in a cAMP-relieved holoenzyme. The existing GO:0004862 row captures that more informative activity. Proposed replacements: cAMP-dependent protein kinase inhibitor activity
GO:0009267 cellular response to starvation	IEA GO_REF:0000117	REMOVE	Summary: Generic ARBA starvation-response transfer to a PKA regulatory subunit. Reason: Bcy1 controls PKA in nutrient and stress signaling, but this broad starvation response row is not supported by a specific Candida assay and does not capture Bcy1's direct work in the PKA holoenzyme.
GO:0009267 cellular response to starvation	IMP PMID:14523129 Integrative, multifunctional plasmids for hypha-specific or ...	UNDECIDED	Summary: The cached plasmid paper is abstract-only. Its abstract reports BCY1-overexpression effects on germ tube formation and filamentation, but no starvation experiment. Reason: Full text was not available in the cache, and the accessible abstract does not explain how BCY1 was assayed in cellular response to starvation. Following the experimental-annotation policy, this row is left unresolved rather than removed. Supporting Evidence: PMID:14523129 Strains overexpressing BCY1 from the ENO1 promoter were inhibited in germ tube formation and filamentation in both liquid and solid media
GO:0010494 cytoplasmic stress granule	IDA PMID:39998251 Exploring the differential localization of protein kinase A ...	KEEP AS NON CORE	Summary: Functional Bcy1-GFP colocalized with the stress-granule marker Pab1-mScarlet in response to elevated temperature. Reason: This is a direct conditional localization of Bcy1 during heat stress. It is retained as non-core because the constitutive PKA regulatory subunit activity is mainly cytosolic. Supporting Evidence: PMID:39998251 All three PKA subunits were associated with Pab1-mSc in response to elevated temperature
GO:0010603 regulation of cytoplasmic mRNA processing body assembly	IEA GO_REF:0000107	REMOVE	Summary: Ensembl Compara transfer from S. cerevisiae Bcy1 to a P-body assembly process. C. albicans Bcy1 localizes to P-bodies after heat stress, but no direct assembly-regulation activity has been shown. Reason: The Candida evidence supports P-body localization of PKA subunits during thermal stress, not direct Bcy1 regulation of P-body assembly. This row is an over-transfer of a downstream S. cerevisiae process. Supporting Evidence: PMID:39998251 PKA subunits are associated with P-bodies in response to thermal insults
GO:0016020 membrane	IEA GO_REF:0000117	TOO GENERAL	Summary: ARBA generic membrane annotation to a soluble PKA regulatory subunit. The direct Candida vacuolar-membrane pool is carbon-source-specific and already represented by an independent IDA row. Reason: Bcy1 is not a generic membrane protein; it is soluble and mainly cytosolic. A conditional subpopulation is enriched around the vacuolar membrane during growth on glycerol, but that specific location is already covered by the direct Candida vacuolar-membrane IDA annotation. TOO_GENERAL rather than REMOVE: vacuolar membrane, kept in this review, entails this term, so the claim is true but less informative. Supporting Evidence: PMID:39998251 Tpk2 and Bcy1, but not Tpk1, were enriched around the vacuolar membrane
GO:0030447 filamentous growth	IMP PMID:14523129 Integrative, multifunctional plasmids for hypha-specific or ...	MODIFY	Summary: BCY1 overexpression inhibited germ tube formation and filamentation. The existing broad filamentous growth annotation should be scoped to Bcy1's negative regulatory role. Reason: Bcy1 is not a structural participant in hyphal extension; it restrains the cAMP-PKA pathway that activates hyphal transcriptional programs. The more informative child term, negative regulation of filamentous growth, is already present and directly supported by BCY1 overexpression, bcy1-deletion, and high-iron BCY1-overexpression phenotypes. Proposed replacements: negative regulation of filamentous growth Supporting Evidence: PMID:14523129 Strains overexpressing BCY1 from the ENO1 promoter were inhibited in germ tube formation and filamentation in both liquid and solid media PMID:28105026 Deletion of BCY1 in C. albicans leads to multiple cellular morphologies and hyperfilamentation in certain media PMID:42506221 Supporting this, overexpression of Bcy1 blocked iron-induced hyphal formation
GO:0030552 cAMP binding	IBA GO_REF:0000033	ACCEPT	Summary: PAINT places cAMP binding at PTHR11635 root node PTN004280545, and the Q9HEW1 sequence carries two cyclic-nucleotide-binding domains. Reason: cAMP binding is a conserved core molecular function of PKA regulatory subunits and is the ligand-binding activity that relieves Bcy1 inhibition of the Tpk catalytic subunits. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN004280545 · PTN004280545 SUPPORTS TRANSFER PAINT places cAMP binding on the root of PTHR11635; Q9HEW1 retains both cyclic-nucleotide-binding domains. Supporting Evidence: PMID:9523695 Photoaffinity labeling with 8-azido-[32P]cAMP of crude extracts from yeast and mycelial cells strongly suggests that only one type of R subunit is present in the fungus
GO:0034236 protein kinase A catalytic subunit binding	IBA GO_REF:0000033	ACCEPT	Summary: PAINT places PKA catalytic-subunit binding at PTHR11635 root node PTN004280545, and Candida Bcy1 coimmunoprecipitated with Tpk1-GFP. Reason: Catalytic-subunit binding is a core conserved PKA regulatory-subunit activity and was directly demonstrated in C. albicans for Bcy1 and Tpk1. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN004280545 · PTN004280545 SUPPORTS TRANSFER PAINT places catalytic-subunit binding on the PKA regulatory-subunit root; C. albicans Bcy1 directly binds the Tpk1 catalytic subunit. Supporting Evidence: PMID:14871949 Coimmunoprecipitation of Tpk1-GFP with Bcy1p in ASM1 and ASM2 strongly suggests interaction of the two proteins inside the cell.
GO:0034605 cellular response to heat	IMP PMID:19391100 Catalytic isoforms Tpk1 and Tpk2 of Candida albicans PKA hav...	KEEP AS NON CORE	Summary: An abstract-only mutant study reported that heterozygous and homozygous BCY1 mutants were highly sensitive to heat treatment. Reason: The direct heat-sensitivity phenotype is retained, but as a conditional stress phenotype of dysregulated PKA rather than Bcy1's core molecular role. Supporting Evidence: PMID:19391100 were highly sensitive to heat treatment PMID:39998251 hyperactivation of PKA is detrimental during these environmental stresses
GO:0042149 cellular response to glucose starvation	IEA GO_REF:0000107	REMOVE	Summary: Ensembl Compara transfer from S. cerevisiae Bcy1 to a glucose-starvation response term. Reason: Candida Bcy1 is a PKA regulatory subunit, and functional Bcy1-GFP does respond to carbon source by accompanying Tpk2 to the vacuolar membrane in glycerol. That does not establish a direct Bcy1 role in the cellular response to glucose starvation process transferred from S. cerevisiae. Supporting Evidence: PMID:39998251 Tpk2 and Bcy1 localize to the vacuolar membrane when C. albicans utilize an alternative carbon source such as glycerol
GO:0042802 identical protein binding	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: Ensembl Compara transfers the S. cerevisiae Bcy1 homodimerization row. PKA holoenzymes contain two regulatory subunits, so R-subunit dimerization is likely, but the generic identical protein binding term is less informative than the accepted PKA regulatory activity and complex rows. Reason: Retained as a plausible non-core homodimerization inference for a PKA regulatory subunit. The direct functional annotations to PKA inhibitor activity, cAMP binding, catalytic-subunit binding, and PKA complex membership are the informative core assertions. Supporting Evidence: PMID:9523695 two regulatory (R) subunits of 64 kDa
GO:0045944 positive regulation of transcription by RNA polymerase II	IEA GO_REF:0000107	REMOVE	Summary: Ensembl Compara transfer from S. cerevisiae Bcy1 to a broad transcription-regulation term. Reason: Bcy1 gates PKA signaling and thereby affects transcriptional programs downstream of Tpk/Efg1, but Bcy1 is not itself a direct RNA polymerase II transcriptional regulator in C. albicans.
GO:0046580 negative regulation of Ras protein signal transduction	IEA GO_REF:0000107	MODIFY	Summary: Ensembl Compara transfer from S. cerevisiae to a Ras-signaling feedback term. Candida Bcy1's conserved direct role is downstream of Ras/Cyr1, as the PKA regulatory subunit required for cAMP responsiveness and for restraining Tpk catalytic activity before cAMP binding. Reason: In C. albicans, Ras1 stimulates Cyr1 upstream of the cAMP-PKA holoenzyme, while Bcy1 binds Tpk catalytic subunits to restrain PKA activity until cAMP binding releases them. The transferred Ras feedback term assigns Bcy1 to the wrong upstream process and should be replaced by cAMP/PKA signal transduction plus Bcy1's direct negative regulation of that pathway. Proposed replacements: cAMP/PKA signal transduction negative regulation of cAMP/PKA signal transduction Supporting Evidence: PMID:14871949 protein kinase A activity in the bcy1 tpk2 mutant was independent of the presence of cAMP PMID:42506221 Supporting this, overexpression of Bcy1 blocked iron-induced hyphal formation
GO:0060258 negative regulation of filamentous growth	IMP PMID:14523129 Integrative, multifunctional plasmids for hypha-specific or ...	KEEP AS NON CORE	Summary: BCY1 overexpression inhibited germ tube formation and filamentation, bcy1-null cells hyperfilamented in several media, and forced BCY1 expression blocked Ras1-independent, iron-induced hyphal formation. Reason: Bcy1's molecular role is to bind cAMP and inhibit Tpk catalytic subunits; negative regulation of filamentation is a major Candida-specific outcome of that PKA gating and is retained as non-core. Supporting Evidence: PMID:14523129 Strains overexpressing BCY1 from the ENO1 promoter were inhibited in germ tube formation and filamentation in both liquid and solid media PMID:28105026 Deletion of BCY1 in C. albicans leads to multiple cellular morphologies and hyperfilamentation in certain media PMID:42506221 Supporting this, overexpression of Bcy1 blocked iron-induced hyphal formation
GO:0097271 protein localization to bud neck	IEA GO_REF:0000107	REMOVE	Summary: Ensembl Compara transfer from the S. cerevisiae Bcy1 bud-neck localization pathway. Reason: No direct C. albicans Bcy1 evidence supports a role in bud-neck protein localization. Direct Candida Bcy1-GFP imaging instead found cytosolic, vacuolar-membrane, P-body, and stress-granule pools under the tested conditions. Supporting Evidence: PMID:39998251 PKA subunits are localized to P-bodies, stress granules, and other foci in response to external environmental stresses

Gene Description

Existing Annotations Review

Core Functions

Bcy1 inhibits cAMP-dependent protein kinase activity by binding Tpk catalytic subunits in the cytosolic PKA holoenzyme, keeping cAMP-PKA signaling restrained until cAMP binding releases active catalytic subunits.

References

Suggested Questions for Experts

Suggested Experiments

📚 Additional Documentation

Notes

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