Hsp82 is the stress-inducible cytosolic Hsp90 paralog in S. cerevisiae and shares about 97% amino-acid identity with the constitutively expressed Hsc82. It is a homodimeric ATP-dependent molecular chaperone that promotes late-stage folding, activation, and structural maintenance of selected client proteins, including the MAPKKK Ste11 and transcriptional regulators. ATP binding, nucleotide-state exchange, conformational transitions, and cochaperones such as Sti1, Aha1, Cdc37, and Sba1 together control client loading, maturation, and release. Hsp82 is expressed at low abundance under nonstress conditions, is strongly induced by heat, and is more thermally stable than Hsc82. It is predominantly cytosolic during vegetative growth and can accumulate in the nucleus during quiescence and sporulation.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0006457 protein folding | IBA GO_REF:0000033 | ACCEPT | Summary: HSP82/Hsp90 is a well-established protein folding chaperone. IBA annotation is consistent with the known function of this conserved chaperone family across eukaryotes. Falcon deep research frames Hsp82 as a selective proteostasis hub that assists late-stage folding, activation, and stability of specific client proteins rather than acting as a general chaperone for all misfolded proteins. Reason: Protein folding is a core biological process for Hsp90. UniProt describes HSP82 as a "Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins." Multiple IMP and IDA evidence codes confirm involvement in selective client-protein folding (PMID:10564510, PMID:9371781). Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000163527 · PAINT Hsp90 family node SUPPORTS TRANSFER The PAINT node captures the conserved Hsp90 ATP-binding, ATPase, and dimeric foldase cycle; Hsp82 remains in this cytosolic Hsp90 clade and retains the core mechanism. Supporting Evidence: file:yeast/HSP82/HSP82-deep-research-falcon.md Hsp82 (Hsp90) is an **ATP-dependent molecular chaperone** that assists the **late-stage folding, activation, and stability** of a large set of specific file:yeast/HSP82/HSP82-deep-research-falcon.md Hsp90/Hsp82 is best understood as a **proteostasis hub** rather than a general chaperone for all misfolded proteins |
| GO:0016887 ATP hydrolysis activity | IBA GO_REF:0000033 | ACCEPT | Summary: HSP82 has well-characterized ATPase activity that regulates its conformational chaperone cycle. The IBA annotation is correct. Falcon deep research places ATP hydrolysis within the dimeric open/closed conformational cycle, noting that the constitutive paralog Hsc82 has somewhat higher ATPase activity than Hsp82 (~1.3-fold at 30C, ~1.6-fold at 37C), with kinetic differences mapping to N-terminal-domain substitutions near the nucleotide pocket. Reason: ATP hydrolysis and nucleotide exchange are conserved features of the Hsp90 cycle and ATPase activity is directly demonstrated for yeast Hsp90 (PMID:12235160). The activity annotation does not require the stronger claim that hydrolysis rate alone determines every essential in vivo function. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000163527 · PAINT Hsp90 family node SUPPORTS TRANSFER The PAINT node captures the conserved Hsp90 ATP-binding, ATPase, and dimeric foldase cycle; Hsp82 remains in this cytosolic Hsp90 clade and retains the core mechanism. Supporting Evidence: file:yeast/HSP82/HSP82-deep-research-falcon.md Client loading, conformational closing, ATP hydrolysis/nucleotide exchange, and reopening are **regulated by co-chaperones** that bind distinct surfaces and bias the timing of transitions file:yeast/HSP82/HSP82-deep-research-falcon.md Hsc82 exhibits **higher ATPase activity** than Hsp82 at both 30°C and 37°C in comparative assays, and kinetic differences map largely to N-terminal-domain substitutions near the nucleotide pocket |
| GO:0032991 protein-containing complex | IBA GO_REF:0000033 | MARK AS OVER ANNOTATED | Summary: HSP82 forms Hsp90 dimers and many co-chaperone/client assemblies, but the generic protein-containing complex term does not identify a biologically meaningful assembly. Reason: Hsp82 genuinely participates in homodimers and specific client/co-chaperone complexes, but GO:0032991 is too broad to convey any of those assemblies. The more informative annotation is ATP-dependent protein folding chaperone activity together with experimentally supported dimerization. The full-length Hsp82-ATP-analogue-Sba1 crystal structure preserves the concrete complex evidence even though no specific complex term is proposed here. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN000163629 · PAINT Hsp90 family node SUPPORTS TRANSFER Hsp90 proteins genuinely form dimers and client/co-chaperone assemblies, but the propagated protein-containing complex term is too generic to identify any such assembly. Supporting Evidence: PMID:16625188 Here we present the crystal structure of full-length yeast Hsp90 in complex with an ATP analogue and the co-chaperone p23/Sba1. file:yeast/HSP82/HSP82-deep-research-falcon.md Yeast has ~14 Hsp90 co-chaperones (diverse domain architectures) that **target clients**, **modulate ATPase activity**, and **stabilize or destabilize** conformational states |
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | MARK AS OVER ANNOTATED | Summary: The IBA transfers plasma-membrane localization from other Hsp90 descendants, whereas direct imaging identifies Hsp82 as a highly abundant cytosolic protein. Reason: HSP82 is an abundant soluble cytosolic chaperone. Targeted GFP imaging showed a prominent cytosolic distribution, and the retrieved literature provides no evidence for a stable functional plasma-membrane pool in budding yeast. Propagation Review Root cause: PROPAGATION BAD Failure modes: COMPARTMENT OR COMPLEX MISMATCH Sources checked: PANTHER:PTN000163629 · PAINT Hsp90 family node SUPPORTS SOURCE BUT NOT TARGET Plasma-membrane localization may occur for some Hsp90 descendants, but direct imaging places this abundant soluble yeast isoform in the cytosol and does not establish membrane residence. Supporting Evidence: PMID:27385335 Each of these candidates (Cdc19, Gpp1, Hsp82, Pgk1, and Tpi1), when expressed as a C-terminally GFP-tagged derivative from its endogenous promoter at its native chromosomal locus, exhibited a very prominent cytosolic distribution |
| GO:0005524 ATP binding | IBA GO_REF:0000033 | ACCEPT | Summary: HSP82 binds ATP as part of its chaperone cycle. Well-established by crystallography. Reason: ATP binding is essential for Hsp90 function. Multiple crystal structures show ATP/ADP binding (PDB:1AM1, 1AMW, 2CG9). UniProt documents extensive ATP binding site residues. The functional cycle is linked to ATP binding and hydrolysis. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000163527 · PAINT Hsp90 family node SUPPORTS TRANSFER The PAINT node captures the conserved Hsp90 ATP-binding, ATPase, and dimeric foldase cycle; Hsp82 remains in this cytosolic Hsp90 clade and retains the core mechanism. Supporting Evidence: PMID:40691164 a role of ATP in Hsp90 function is structural: it is a severable linker that facilitates both the formation and dissociation of the closed clamp |
| GO:0005829 cytosol | IBA GO_REF:0000033 | ACCEPT | Summary: HSP82 is a cytosolic protein. IBA annotation is correct. Falcon deep research confirms that cytosolic Hsp90 (Hsp82/Hsc82) is broadly distributed during vegetative growth. Reason: Consistent with IDA evidence for cytoplasm localization (PMID:32920053, PMID:27385335) and HDA data (PMID:11914276, PMID:14562095). Cytosol is the expected localization for Hsp90. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000163629 · PAINT Hsp90 family node SUPPORTS TRANSFER The PAINT node captures the cytosolic eukaryotic Hsp90 clade; Hsp82 is the stress-inducible budding-yeast member and retains cytosolic client maturation and stabilization capacity. Supporting Evidence: file:yeast/HSP82/HSP82-deep-research-falcon.md Cytosolic Hsp90 (Hsp82/Hsc82) is broadly distributed during vegetative growth |
| GO:0050821 protein stabilization | IBA GO_REF:0000033 | ACCEPT | Summary: HSP82 stabilizes client proteins as part of its chaperone function. IBA annotation is appropriate. Falcon deep research describes Hsp82 as assisting the late-stage folding, activation, and stability of a defined set of client proteins. Reason: Protein stabilization is a core function of Hsp90. IMP evidence shows HSP82 is required for protein maturation (PMID:27068472). UniProt states it "promotes the maturation, structural maintenance and proper regulation of specific target proteins." Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000163629 · PAINT Hsp90 family node SUPPORTS TRANSFER The PAINT node captures the cytosolic eukaryotic Hsp90 clade; Hsp82 is the stress-inducible budding-yeast member and retains cytosolic client maturation and stabilization capacity. Supporting Evidence: file:yeast/HSP82/HSP82-deep-research-falcon.md Hsp82 (Hsp90) is an **ATP-dependent molecular chaperone** that assists the **late-stage folding, activation, and stability** of a large set of specific |
| GO:0034605 cellular response to heat | IBA GO_REF:0000033 | ACCEPT | Summary: HSP82 is the heat-inducible Hsp90 isoform, centrally involved in heat stress response. Falcon deep research provides quantitative support: Hsp82 is very low at 25-30C and induced at 37C to levels similar to the constitutive Hsc82 paralog, and Hsp82 is more thermally stable than Hsc82 (Tm ~60.4C vs 57.1C), consistent with a stress-specialized role. Reason: HSP82 is named as a heat shock protein precisely because it is induced by heat stress. UniProt confirms it is "required for growth at high temperatures" (PMID:2674684). The gene name itself (HSP82 = Heat Shock Protein 82) reflects this core function. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000163629 · PAINT Hsp90 family node SUPPORTS TRANSFER The PAINT node captures the cytosolic eukaryotic Hsp90 clade; Hsp82 is the stress-inducible budding-yeast member and retains cytosolic client maturation and stabilization capacity. Supporting Evidence: file:yeast/HSP82/HSP82-deep-research-falcon.md **Hsp82 is very low at 25–30°C and induced at 37°C to levels similar to Hsc82**, consistent with a stress-specialized role file:yeast/HSP82/HSP82-deep-research-falcon.md Hsp82 is **more thermally stable** than Hsc82 (Tm ~60.4°C vs 57.1°C) |
| GO:0048471 perinuclear region of cytoplasm | IBA GO_REF:0000033 | MARK AS OVER ANNOTATED | Summary: The IBA transfers a perinuclear-cytoplasm localization claim within the cytosolic Hsp90 family, but direct HSP82 evidence supports diffuse cytosol and condition-dependent nuclear accumulation rather than stable perinuclear enrichment. Reason: Hsp82 is an abundant soluble cytosolic chaperone. Perinuclear localization may occur for some Hsp90 descendants or specialized contexts, but the HSP82 literature recovered here does not establish a stable functional perinuclear pool in budding yeast. Propagation Review Root cause: PROPAGATION BAD Failure modes: COMPARTMENT OR COMPLEX MISMATCH Sources checked: PANTHER:PTN000163629 · PAINT Hsp90 family node SUPPORTS SOURCE BUT NOT TARGET The cytosolic-Hsp90 node does not justify stable perinuclear enrichment for every descendant; direct HSP82 imaging supports diffuse cytosol and condition-dependent nuclear accumulation instead. |
| GO:0000492 box C/D snoRNP assembly | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: ARBA machine learning prediction for snoRNP assembly involvement. Supported by IMP evidence. Reason: Supported by IMP evidence (PMID:18268103) which showed Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex activity that regulates snoRNA accumulation. This is a legitimate but secondary function of Hsp90, mediated through its general chaperone role on client proteins in the R2TP pathway. Supporting Evidence: PMID:18268103 Together with the Tah1 cofactor, Hsp90 functions to stabilize Pih1. As a consequence, the chaperone is shown to affect box C/D accumulation and maintenance, especially under stress conditions. |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: IEA annotation for cytoplasm from UniProt subcellular location mapping. Correct. Reason: Consistent with multiple IDA and HDA evidence for cytoplasmic localization. |
| GO:0006457 protein folding | IEA GO_REF:0000120 | ACCEPT | Summary: IEA annotation for protein folding. Redundant with IBA but correct. Reason: Consistent with IBA and experimental annotations for protein folding involvement. |
| GO:0016887 ATP hydrolysis activity | IEA GO_REF:0000120 | ACCEPT | Summary: IEA annotation for ATP hydrolysis activity. Redundant with IBA and IDA but correct. Reason: Consistent with IBA and IDA (PMID:12235160) annotations for ATPase activity. |
| GO:0043248 proteasome assembly | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: ARBA prediction for proteasome assembly involvement. Supported by IDA/IMP evidence. Reason: Supported by experimental evidence (IDA and IMP, PMID:12853471). HSP82 assists in proteasome assembly as one of its client-dependent functions. Not a core function of HSP82 per se, but a legitimate downstream consequence of its chaperone activity. Supporting Evidence: PMID:12853471 Herein we report a novel function for Hsp90 in the ATP-dependent assembly of the 26S proteasome. |
| GO:0140662 ATP-dependent protein folding chaperone | IEA GO_REF:0000002 | ACCEPT | Summary: IEA annotation from InterPro for ATP-dependent protein folding chaperone. This is the correct and most informative molecular function term for HSP82. Falcon deep research describes Hsp82 as a dimeric chaperone cycling between an open (C-terminally dimerized) state and an ATP-induced closed state with additional N-terminal contacts. Reason: GO:0140662 is the ideal molecular function term for HSP82/Hsp90. It captures both the ATP dependence and the protein folding chaperone activity. HSP82 binds to client proteins and assists their folding through an ATP-dependent conformational cycle. This should be considered the primary MF annotation for HSP82. Supporting Evidence: file:yeast/HSP82/HSP82-deep-research-falcon.md Yeast Hsp90 (Hsp82/Hsc82) is a **dimeric** chaperone cycling between file:yeast/HSP82/HSP82-deep-research-falcon.md an **ATP-induced closed** state with additional N-terminal contacts |
| GO:0005515 protein binding | IPI PMID:11805837 Systematic identification of protein complexes in Saccharomy... | REMOVE | Summary: Cns1 was recovered with Hsp82 in a proteome-scale AP-MS survey, but the cached abstract does not establish the TPR-domain contact made by Cns1. Reason: Cns1 is a bona fide TPR co-chaperone, but this row comes from a high-throughput complex-discovery paper rather than a domain-mapping study. Remove the generic protein-binding annotation and keep the domain-specific Cns1 inference on the direct PMID:9819422 row. |
| GO:0005515 protein binding | IPI PMID:12604615 Aha1 binds to the middle domain of Hsp90, contributes to cli... | REMOVE | Summary: The cached abstract for this Aha1/Hch1 study does not establish Sti1-TPR binding. Reason: Sti1 is a bona fide Hsp90 TPR co-chaperone, but this GOA/IntAct row should not be narrowed to GO:0030911 unless the cited paper supports the TPR-domain contact. The cached abstract names Aha1 and Hch1 as the characterized Hsp90-binding partners. |
| GO:0005515 protein binding | IPI PMID:14729968 The ctf13-30/CTF13 genomic haploinsufficiency modifier scree... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:15102838 A novel mode of chaperone action: heme activation of Hap1 by... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:15766533 Navigating the chaperone network: an integrative map of phys... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:15879519 A two-hybrid screen of the yeast proteome for Hsp90 interact... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:16407978 The phosphatase Ppt1 is a dedicated regulator of the molecul... | REMOVE | Summary: The Ppt1 paper directly supports TPR-domain binding for the Ppt1 row, but not for this Sti1 row in its cached abstract. Reason: Sti1 is a bona fide Hsp90 TPR co-chaperone, but the cached evidence in this reference is specific for the Ppt1 TPR-domain attachment to Hsp90 and should not be over-read as direct support for a domain-level Sti1 annotation. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | REMOVE | Summary: Sti1 was recovered with Hsp82 in a large AP-MS modularity survey, but the cached abstract does not establish TPR-domain binding. Reason: The supporting interaction may be real, but this proteome-scale screen is not a domain-mapping study for the Hsp82-Sti1 interface. Remove the generic GO:0005515 assertion rather than inferring GO:0030911 from the partner identity alone. |
| GO:0005515 protein binding | IPI PMID:16625188 Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed cha... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:18268103 Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain ... | MODIFY | Summary: The R2TP study used Sti1 TPR2a as a positive control and showed direct binding to the Hsp82 C-terminal MEEVD-containing fragment. Reason: Replace the generic GO:0005515 row with GO:0030911 TPR domain binding. The cited full text directly maps a Sti1 TPR2a-domain interaction to the Hsp82 MC fragment and excludes the NM fragment, matching the C-terminal MEEVD recognition used by TPR co-chaperones. Proposed replacements: TPR domain binding Supporting Evidence: PMID:18268103 As a positive control, the TPR2a domain from Sti1 (Fig. 1 A) interacted with Hsp82-MC but not with Hsp82-NM (Fig. 1 B, right). |
| GO:0005515 protein binding | IPI PMID:18719252 High-quality binary protein interaction map of the yeast int... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:18818696 Structural and functional coupling of Hsp90- and Sgt1-centre... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:18833289 Structural and functional analysis of SGT1-HSP90 core comple... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:21170051 Mixed Hsp90-cochaperone complexes are important for the prog... | REMOVE | Summary: This Sti1-focused paper supports the Hsp90-Sti1 complex in the chaperone cycle, but the cached abstract does not map the interaction to a TPR domain. Reason: Sti1 is a bona fide TPR co-chaperone and this paper directly concerns Hsp90-Sti1 mixed complexes, but the cached text only supports the complex-level interaction. Leave the generic protein-binding annotation removed rather than converting it to GO:0030911 without domain-level evidence from this reference. |
| GO:0005515 protein binding | IPI PMID:21892170 Structural analysis of the interaction between Hsp90 and the... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:23217712 CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abund... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:23396352 Integration of the accelerator Aha1 in the Hsp90 co-chaperon... | REMOVE | Summary: This Aha1/Cpr6-cycle paper mentions Sti1 displacement from Hsp90 but does not map a Sti1 TPR-domain contact in its cached abstract. Reason: The paper supports a role for Aha1 and Cpr6 in displacing Sti1 from Hsp90; that chaperone-cycle context does not by itself turn this GO:0005515 row into a reference-supported TPR domain binding annotation. |
| GO:0005515 protein binding | IPI PMID:24012479 High-resolution structural analysis shows how Tah1 tethers H... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:24794838 Structural basis for phosphorylation-dependent recruitment o... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:37968396 The social and structural architecture of the yeast protein ... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:9817749 In vivo function of Hsp90 is dependent on ATP binding and AT... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:9819422 Cns1 is an essential protein associated with the hsp90 chape... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0042802 identical protein binding | IPI PMID:16625188 Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed cha... | ACCEPT | Summary: HSP82 forms homodimers as part of its functional cycle. The crystal structure (PDB:2CG9) confirms dimerization. Falcon deep research describes yeast Hsp90 as a dimeric chaperone whose open state is C-terminally dimerized, with the conserved co-chaperone-binding motif at the C-terminus. Reason: Homodimerization is essential for Hsp90 function. The crystal structure of the closed chaperone complex (PMID:16625188) directly shows the dimer. This is a core structural feature of Hsp90. Supporting Evidence: file:yeast/HSP82/HSP82-deep-research-falcon.md an **open** state (C-terminally dimerized) and file:yeast/HSP82/HSP82-deep-research-falcon.md **C-terminal dimerization domain** including the conserved co-chaperone-binding motif at the C-terminus |
| GO:0042802 identical protein binding | IPI PMID:18268103 Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain ... | ACCEPT | Summary: Additional evidence for HSP82 homodimerization. Reason: Consistent with known Hsp90 dimerization. Duplicate annotation with different reference is fine. Supporting Evidence: PMID:18268103 Hsp82 eluted at the position of a dimer, whereas Tah1 and Pih1 eluted as monomers. |
| GO:0042802 identical protein binding | IPI PMID:19696785 Hsp90 is regulated by a switch point in the C-terminal domai... | ACCEPT | Summary: HSP82 homodimerization via C-terminal domain switch point study. Reason: C-terminal domain dimerization dynamics are important for the conformational cycle. Mutagenesis of A577 modulates dimerization, ATPase, and client activation. |
| GO:0042802 identical protein binding | IPI PMID:20736353 Dynamics of heat shock protein 90 C-terminal dimerization is... | ACCEPT | Summary: HSP82 C-terminal dimerization dynamics study. Reason: Further confirmation of homodimerization as essential for the conformational cycle. |
| GO:0042802 identical protein binding | IPI PMID:23396352 Integration of the accelerator Aha1 in the Hsp90 co-chaperon... | ACCEPT | Summary: HSP82 homodimerization in context of Aha1 co-chaperone cycle. Reason: Consistent with known Hsp90 dimerization. |
| GO:0042802 identical protein binding | IPI PMID:24794838 Structural basis for phosphorylation-dependent recruitment o... | ACCEPT | Summary: HSP82 homodimerization in Tel2-Hsp90-Pih1 study. Reason: Consistent with known Hsp90 dimerization. |
| GO:0042802 identical protein binding | IPI PMID:31454312 The role of structural pleiotropy and regulatory evolution i... | ACCEPT | Summary: HSP82 homodimerization in paralog heteromer study. Reason: The study's interaction dataset supports self-association, and independent direct size-exclusion evidence confirms that purified Hsp82 is dimeric. The paralog study also addresses HSP82-HSC82 heteromer retention, which is distinct from this identical-protein-binding annotation. Supporting Evidence: PMID:18268103 Hsp82 eluted at the position of a dimer, whereas Tah1 and Pih1 eluted as monomers. |
| GO:0070482 response to oxygen levels | NAS PMID:9632766 Molecular mechanism governing heme signaling in yeast: a hig... | KEEP AS NON CORE | Summary: NAS annotation from ComplexPortal, based on HSP82 involvement in HAP1-mediated heme signaling. Reason: HSP82 forms a complex with HAP1, a transcriptional activator regulated by heme (proxy for oxygen), and Hsp90 function supports HAP1 activation at high heme concentrations. This is a client-dependent function rather than a core response to oxygen levels. Supporting Evidence: PMID:9632766 Our data suggest that this complex contains HAP1 and four other cellular proteins including Hsp82 and Ydj1. PMID:15102838 defective Hsp90 function causes reduced Hap1 activity at high heme concentrations. |
| GO:0005634 nucleus | IDA PMID:32920053 A Single Site Phosphorylation on Hsp82 Ensures Cell Survival... | KEEP AS NON CORE | Summary: IDA evidence for nuclear localization from starvation phosphorylation study. Falcon deep research reinforces a condition-dependent nuclear pool: Hsp90 (with the co-chaperone Sba1/p23) accumulates in the nucleus in quiescent cells (glucose exhaustion) and in sporulating diploids, where nuclear accumulation defects correlate with sporulation/spore-wall defects. Reason: HSP82 is primarily cytoplasmic but a nuclear pool exists, enhanced during starvation, quiescence, and sporulation. The starvation study (PMID:32920053) showed phosphorylation-dependent nuclear localization, and falcon deep research corroborates condition-dependent nuclear accumulation (Tapia & Morano 2010). Nuclear localization remains a regulated, non-core compartment rather than the primary site of action. Supporting Evidence: PMID:32920053 Furthermore, we found that Ppt1 regulates Hsp82 distribution in the cytoplasm and nucleus by dephosphorylating the S485 residue on Hsp82. file:yeast/HSP82/HSP82-deep-research-falcon.md **accumulates in the nucleus in quiescent cells (glucose exhaustion)** and in sporulating diploids |
| GO:0005737 cytoplasm | IDA PMID:32920053 A Single Site Phosphorylation on Hsp82 Ensures Cell Survival... | ACCEPT | Summary: IDA evidence for cytoplasmic localization. Reason: Core localization of HSP82. Consistent with multiple lines of evidence. |
| GO:0016887 ATP hydrolysis activity | IDA PMID:12235160 N-terminal residues regulate the catalytic efficiency of the... | ACCEPT | Summary: Direct assay evidence for ATPase activity of HSP82. Reason: Core molecular function. Direct biochemical analysis showed that Hsp90 variants are impaired in ATP hydrolysis without losing nucleotide binding. Supporting Evidence: PMID:12235160 We show that N-terminal deletion variants of Hsp90 are severely impaired in their ability to hydrolyze ATP. However, nucleotide binding of these constructs is similar to that of the wild type protein. |
| GO:0016887 ATP hydrolysis activity | IMP PMID:27068472 Systematic Mutant Analyses Elucidate General and Client-Spec... | ACCEPT | Summary: Mutant phenotype evidence for ATPase activity from systematic mutant analysis. Reason: Systematic mutational analysis of the ATPase domain linked residues near ATP phosphates to yeast growth and showed client-specific effects on v-Src and glucocorticoid-receptor activation. This complements the direct biochemical ATPase evidence without implying that every client uses an identical mechanism. Supporting Evidence: PMID:27068472 The sensitivity of a position to mutation was strongly influenced by proximity to the phosphates of ATP, indicating that ATPase-driven conformational changes impose stringent physical constraints on Hsp90. |
| GO:0005737 cytoplasm | HDA PMID:11914276 Subcellular localization of the yeast proteome. | ACCEPT | Summary: High-throughput data for cytoplasmic localization. Reason: Consistent with IDA evidence. |
| GO:0005737 cytoplasm | HDA PMID:14562095 Global analysis of protein localization in budding yeast. | ACCEPT | Summary: High-throughput GFP localization data confirming cytoplasm. Reason: Global protein localization study. Consistent with IDA evidence. |
| GO:0005737 cytoplasm | IDA PMID:27385335 Detection of protein-protein interactions at the septin coll... | ACCEPT | Summary: Direct GFP imaging shows Hsp82 in the cytosol, supporting the imported cytoplasm annotation. Reason: GFP imaging of Hsp82 expressed from its endogenous locus directly showed a prominent cytosolic distribution. Cytoplasm is a valid broader parent term, and Hsp82 served as an abundant cytosolic negative control for septin interactions. Supporting Evidence: PMID:27385335 Each of these candidates (Cdc19, Gpp1, Hsp82, Pgk1, and Tpi1), when expressed as a C-terminally GFP-tagged derivative from its endogenous promoter at its native chromosomal locus, exhibited a very prominent cytosolic distribution |
| GO:0051604 protein maturation | IMP PMID:27068472 Systematic Mutant Analyses Elucidate General and Client-Spec... | ACCEPT | Summary: IMP evidence from systematic mutant analysis showing HSP82 is required for protein maturation. Reason: UniProt describes HSP82 as promoting "the maturation, structural maintenance and proper regulation of specific target proteins." Protein maturation is a core function of Hsp90. |
| GO:0000492 box C/D snoRNP assembly | IMP PMID:18268103 Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain ... | KEEP AS NON CORE | Summary: IMP evidence showing Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex for snoRNP assembly. Reason: Hsp90 acts on the R2TP pathway components (Pih1, Tah1) that are required for snoRNP assembly. This is a legitimate client-dependent function but not a core function of HSP82. Supporting Evidence: PMID:18268103 Together with the Tah1 cofactor, Hsp90 functions to stabilize Pih1. As a consequence, the chaperone is shown to affect box C/D accumulation and maintenance, especially under stress conditions. |
| GO:0006458 'de novo' protein folding | IDA PMID:10564510 Contribution of N- and C-terminal domains to the function of... | KEEP AS NON CORE | Summary: PMID:10564510 directly supports non-native-client binding and maturation of selected signaling clients, which is a narrower client-specific subset of de novo protein folding. Reason: The study concerns cofactor-regulated maturation of Hsp90 substrates. Its evidence is consistent with a selective role in folding newly synthesized difficult clients rather than a general role for every nascent polypeptide, so keep the SGD experimental process as a contextual client-maturation annotation and do not duplicate the broader electronic GO:0006457 rows. Supporting Evidence: file:yeast/HSP82/HSP82-deep-research-falcon.md Hsp82 (Hsp90) is an **ATP-dependent molecular chaperone** that assists the **late-stage folding, activation, and stability** of a large set of specific “client” proteins (substrates), including many signaling regulators (notably protein kinases and transcription factors). |
| GO:0006458 'de novo' protein folding | IMP PMID:9371781 In vivo functions of the Saccharomyces cerevisiae Hsp90 chap... | KEEP AS NON CORE | Summary: Mutant evidence shows that Hsp90 supports folding of a restricted difficult-client subset. Reason: Mutant analysis showed that Hsp90 is required for the subset of proteins that have difficulty reaching native conformations, while being dispensable for de novo folding of most proteins. This supports the SGD experimental row as a client-subset process rather than as a core annotation, and it should not be collapsed to the duplicate parent GO:0006457. Supporting Evidence: PMID:9371781 The data suggest that Hsp90 is not required for the de novo folding of most proteins, but it is required for a specific subset of proteins that have greater difficulty reaching their native conformations. |
| GO:0006970 response to osmotic stress | IMP PMID:16487343 The molecular chaperone Hsp90 is required for high osmotic s... | KEEP AS NON CORE | Summary: IMP evidence showing Hsp90 is required for high osmotic stress response. Reason: Hsp90 is required for adaptation to high osmolarity through a Cdc37-dependent pathway parallel to, rather than within, the canonical HOG pathway. This is a legitimate conditional phenotype but secondary to the core chaperone activity. Supporting Evidence: PMID:16487343 Hsp90 is shown to be required for proper adaptation to high osmolarity via a novel signal transduction pathway that operates parallel to the HOG pathway and requires Cdc37p. |
| GO:0032212 positive regulation of telomere maintenance via telomerase | IDA PMID:17954556 The hsp90 molecular chaperone modulates multiple telomerase ... | KEEP AS NON CORE | Summary: IDA evidence for positive regulation of telomere maintenance via telomerase. Reason: Hsp90 modulates multiple telomerase activities. This is a client-dependent function where Hsp90 chaperones telomerase components. Not a core function of HSP82 itself. Supporting Evidence: PMID:17954556 We have found that the yeast Hsp90 homolog Hsp82p promotes both telomerase DNA binding and nucleotide addition properties. |
| GO:0032212 positive regulation of telomere maintenance via telomerase | IMP PMID:17954556 The hsp90 molecular chaperone modulates multiple telomerase ... | KEEP AS NON CORE | Summary: IMP evidence for telomerase regulation. Reason: Complements IDA evidence. Client-dependent function. Supporting Evidence: PMID:17954556 Importantly, telomere length and telomerase telomere occupancy was yeast Hsp90 dependent. |
| GO:0042026 protein refolding | IMP PMID:9371781 In vivo functions of the Saccharomyces cerevisiae Hsp90 chap... | ACCEPT | Summary: IMP evidence for protein refolding activity from in vivo function study. Reason: Protein refolding is a core chaperone function for selected damaged clients rather than a general capacity to reactivate every heat-damaged protein. The in vivo mutant study demonstrated enhanced reactivation of a heat-damaged substrate. Supporting Evidence: PMID:9371781 Under conditions of stress, Hsp90 does not generally protect proteins from thermal inactivation but does enhance the rate at which a heat-damaged protein is reactivated. |
| GO:0043248 proteasome assembly | IDA PMID:12853471 The molecular chaperone Hsp90 plays a role in the assembly a... | KEEP AS NON CORE | Summary: IDA evidence for proteasome assembly involvement. Reason: HSP82 assists in proteasome assembly as a client-dependent function. The chaperone assists proteasome maturation but this is secondary to its core function. Supporting Evidence: PMID:12853471 Herein we report a novel function for Hsp90 in the ATP-dependent assembly of the 26S proteasome. |
| GO:0043248 proteasome assembly | IMP PMID:12853471 The molecular chaperone Hsp90 plays a role in the assembly a... | KEEP AS NON CORE | Summary: IMP evidence for proteasome assembly. Reason: Complements IDA evidence. Client-dependent function. Supporting Evidence: PMID:12853471 Functional loss of Hsp90 using a temperature-sensitive mutant in yeast caused dissociation of the 26S proteasome. |
| GO:0032204 regulation of telomere maintenance | IMP PMID:21829731 HSP90 controls SIR2 mediated gene silencing. | KEEP AS NON CORE | Summary: IMP evidence from CACAO annotation showing HSP90 controls SIR2-mediated gene silencing and telomere maintenance. Reason: HSP90 controls SIR2-mediated gene silencing which affects telomere maintenance. This is another example of a client-dependent function. Secondary to core chaperone activity. |
| GO:0005515 protein binding | IPI PMID:11805837 Systematic identification of protein complexes in Saccharomy... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:11805837 Systematic identification of protein complexes in Saccharomy... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:11805837 Systematic identification of protein complexes in Saccharomy... | REMOVE | Summary: Ppt1 was recovered with Hsp82 in a proteome-scale AP-MS survey, but the cached abstract does not establish the Ppt1 TPR-domain contact. Reason: Ppt1 is a bona fide Hsp90 TPR co-chaperone and phosphatase, but this row is supported by a high-throughput complex-discovery paper rather than the focused Ppt1 study. Remove the generic GO:0005515 row and retain the domain-specific replacement on the direct PMID:16407978 row. |
| GO:0005515 protein binding | IPI PMID:11805837 Systematic identification of protein complexes in Saccharomy... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:11805837 Systematic identification of protein complexes in Saccharomy... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:12604615 Aha1 binds to the middle domain of Hsp90, contributes to cli... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:15766533 Navigating the chaperone network: an integrative map of phys... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:15766533 Navigating the chaperone network: an integrative map of phys... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:15766533 Navigating the chaperone network: an integrative map of phys... | REMOVE | Summary: Sti1 was detected in an Hsp90-centered proteomic/genomic interaction map, but this high-throughput row does not establish a domain-level TPR contact. Reason: The cited study mapped a broad Hsp90 physical and genetic network and identified many cofactors and substrates. It is useful interaction evidence, but it is not sufficient to replace GO:0005515 with GO:0030911 for every recovered TPR-containing co-chaperone. |
| GO:0005515 protein binding | IPI PMID:15766533 Navigating the chaperone network: an integrative map of phys... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:15766533 Navigating the chaperone network: an integrative map of phys... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:15766533 Navigating the chaperone network: an integrative map of phys... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:15766533 Navigating the chaperone network: an integrative map of phys... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:15766533 Navigating the chaperone network: an integrative map of phys... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:15766533 Navigating the chaperone network: an integrative map of phys... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:15766533 Navigating the chaperone network: an integrative map of phys... | REMOVE | Summary: Cns1 was detected in an Hsp90-centered proteomic/genomic interaction map, but this high-throughput row does not establish a domain-level TPR contact. Reason: The cited study mapped a broad Hsp90 physical and genetic network. Remove this generic GO:0005515 row rather than converting it to GO:0030911 from partner identity alone; the focused Cns1 paper provides a better source for the domain-specific inference. |
| GO:0005515 protein binding | IPI PMID:15766533 Navigating the chaperone network: an integrative map of phys... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:15766533 Navigating the chaperone network: an integrative map of phys... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:15766533 Navigating the chaperone network: an integrative map of phys... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:15766533 Navigating the chaperone network: an integrative map of phys... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:15766533 Navigating the chaperone network: an integrative map of phys... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:15766533 Navigating the chaperone network: an integrative map of phys... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:15766533 Navigating the chaperone network: an integrative map of phys... | REMOVE | Summary: Ppt1 was detected in an Hsp90-centered proteomic/genomic interaction map, but this high-throughput row does not establish a domain-level TPR contact. Reason: The cited study mapped a broad Hsp90 physical and genetic network. Remove this generic GO:0005515 row rather than converting it to GO:0030911 from partner identity alone; the direct Ppt1 phosphatase paper provides the support for a TPR-specific replacement. |
| GO:0005515 protein binding | IPI PMID:15766533 Navigating the chaperone network: an integrative map of phys... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:15766533 Navigating the chaperone network: an integrative map of phys... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:15766533 Navigating the chaperone network: an integrative map of phys... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:15766533 Navigating the chaperone network: an integrative map of phys... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:15766533 Navigating the chaperone network: an integrative map of phys... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:15766533 Navigating the chaperone network: an integrative map of phys... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:15879519 A two-hybrid screen of the yeast proteome for Hsp90 interact... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:15879519 A two-hybrid screen of the yeast proteome for Hsp90 interact... | REMOVE | Summary: Sti1 was recovered in a yeast two-hybrid screen for Hsp90 interactors, but the cached paper focuses on Slt2/Mpk1 and does not map a Sti1 TPR-domain contact. Reason: This screen used a mutant Hsp90 designed to stabilize transient client complexes and directly characterized MAPK client binding. The Sti1 hit is not enough, from the cached text, to support replacing this IntAct GO:0005515 row with GO:0030911. |
| GO:0005515 protein binding | IPI PMID:15879519 A two-hybrid screen of the yeast proteome for Hsp90 interact... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:15879519 A two-hybrid screen of the yeast proteome for Hsp90 interact... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:15879519 A two-hybrid screen of the yeast proteome for Hsp90 interact... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:15879519 A two-hybrid screen of the yeast proteome for Hsp90 interact... | REMOVE | Summary: Cns1 was recovered in a yeast two-hybrid screen for Hsp90 interactors, but the cached paper focuses on Slt2/Mpk1 and does not map a Cns1 TPR-domain contact. Reason: This screen used a mutant Hsp90 designed to stabilize transient client complexes and directly characterized MAPK client binding. Remove this generic row rather than inferring GO:0030911 from a screen hit when the focused Cns1 paper better supports that interaction. |
| GO:0005515 protein binding | IPI PMID:15879519 A two-hybrid screen of the yeast proteome for Hsp90 interact... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:15879519 A two-hybrid screen of the yeast proteome for Hsp90 interact... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:15879519 A two-hybrid screen of the yeast proteome for Hsp90 interact... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:15879519 A two-hybrid screen of the yeast proteome for Hsp90 interact... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:15879519 A two-hybrid screen of the yeast proteome for Hsp90 interact... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:16407978 The phosphatase Ppt1 is a dedicated regulator of the molecul... | MODIFY | Summary: The Ppt1 study directly supports binding by Hsp82 to a TPR-domain protein phosphatase. Reason: Replace the generic GO:0005515 row with GO:0030911 TPR domain binding and GO:0019903 protein phosphatase binding. The cited abstract states that Ppt1 directly dephosphorylates Hsp90 and that this activity requires direct TPR-domain attachment to Hsp90. Proposed replacements: TPR domain binding protein phosphatase binding Supporting Evidence: PMID:16407978 We show that purified Ppt1 specifically dephosphorylates Hsp90. This activity requires Hsp90 to be directly attached to Ppt1 via its TPR domain. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | REMOVE | Summary: Ppt1 was recovered with Hsp82 in a large AP-MS modularity survey, but the cached abstract does not establish TPR-domain binding or protein-phosphatase binding. Reason: Ppt1 is a bona fide Hsp90 TPR co-chaperone and phosphatase, but this proteome-scale screen is not the source that demonstrates those molecular functions for Hsp82. Remove the generic GO:0005515 row and retain the specific replacement on the direct PMID:16407978 row. |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:18268103 Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain ... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:18268103 Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain ... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:18719252 High-quality binary protein interaction map of the yeast int... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:21170051 Mixed Hsp90-cochaperone complexes are important for the prog... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:23396352 Integration of the accelerator Aha1 in the Hsp90 co-chaperon... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:23396352 Integration of the accelerator Aha1 in the Hsp90 co-chaperon... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:23396352 Integration of the accelerator Aha1 in the Hsp90 co-chaperon... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:23396352 Integration of the accelerator Aha1 in the Hsp90 co-chaperon... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:24012479 High-resolution structural analysis shows how Tah1 tethers H... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:24794838 Structural basis for phosphorylation-dependent recruitment o... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:37968396 The social and structural architecture of the yeast protein ... | REMOVE | Summary: Sti1 was recovered in the 2023 yeast interactome, but this global AP-MS row does not establish a Sti1 TPR-domain contact. Reason: The supporting interaction may be real, but the row is another high-throughput IntAct protein-binding import. The cached paper presents a global interactome and does not justify a GO:0030911 replacement for this specific TPR co-chaperone edge. |
| GO:0005515 protein binding | IPI PMID:37968396 The social and structural architecture of the yeast protein ... | REMOVE | Summary: Ppt1 was recovered in the 2023 yeast interactome, but this global AP-MS row does not establish TPR-domain binding or protein-phosphatase binding. Reason: The supporting interaction may be real, but the row is another high-throughput IntAct protein-binding import. Remove the generic GO:0005515 annotation and use the focused PMID:16407978 row for the specific Ppt1 molecular-function replacements. |
| GO:0005515 protein binding | IPI PMID:37968396 The social and structural architecture of the yeast protein ... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:9819422 Cns1 is an essential protein associated with the hsp90 chape... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005515 protein binding | IPI PMID:9819422 Cns1 is an essential protein associated with the hsp90 chape... | REMOVE | Summary: The Cns1 paper establishes a Cns1-Hsp90 carboxy-terminal interaction, but not this separate Sti1 edge in its cached abstract. Reason: Sti1 is a bona fide Hsp90 TPR co-chaperone, but this row should not be narrowed to GO:0030911 based on a paper whose abstract directly supports Cns1 instead. Remove the generic GO:0005515 row rather than carrying over the Cns1-specific domain inference. |
| GO:0005515 protein binding | IPI PMID:9819422 Cns1 is an essential protein associated with the hsp90 chape... | MODIFY | Summary: The foundational Cns1 paper supports interaction between Cns1 and the Hsp90 carboxy terminus and identifies Cns1 as a TPR-containing Hsp90-complex component. Reason: Replace the generic GO:0005515 row with GO:0030911 TPR domain binding. Cns1 is a TPR-containing co-chaperone, and the cited abstract reports interaction between Cns1 and the Hsp90 carboxy terminus, consistent with the MEEVD-directed TPR interaction used by Hsp90 co-chaperones. Proposed replacements: TPR domain binding Supporting Evidence: PMID:9819422 Interaction between Cns1 and the carboxy terminus of Hsp90 was also shown by two-hybrid analysis. |
| GO:0005515 protein binding | IPI PMID:9819422 Cns1 is an essential protein associated with the hsp90 chape... | REMOVE | Summary: Hsp82 physical associations captured by IntAct are useful interaction evidence, but the generic protein-binding label is uninformative for this ATP-dependent chaperone. Reason: The supporting interaction may be real, but GO:0005515 does not describe Hsp82's ATP-dependent chaperone activity, co-chaperone specificity, or a specific client-maturation function; remove the generic binding annotation rather than treating it as over-annotation. |
| GO:0005524 ATP binding | IEA GO_REF:0000002 | ACCEPT | Summary: InterPro2GO annotation of ATP binding through the Hsp90-family ATPase domain; this is a correct component of the Hsp82 chaperone cycle. Reason: Hsp82 binds ATP in its N-terminal GHKL ATPase domain, and ATP binding helps drive the closed-clamp conformation around clients. The 2025 nucleotide-pocket mutational analysis further supports a structural role for ATP as a linker stabilizing the closed clamp. Supporting Evidence: PMID:40691164 ATP is a linker that physically tethers the N and M domains and stabilizes closing |
| GO:0019899 enzyme binding | EXP PMID:28278223 The structure of FKBP38 in complex with the MEEVD tetratrico... | MODIFY | Summary: The FKBP38 study used the yeast Hsp90 C-terminal MEEVD-containing fragment and showed binding to a TPR-domain carboxylate clamp, but GO:0019899 enzyme binding is too generic for this activity. Reason: The assayed FKBP92-380 construct contains a PPIase domain, but the Hsp90 contact is through the C-terminal MEEVD peptide and the FKBP8 TPR domain. Replace the generic enzyme-binding label with GO:0030911 TPR domain binding, which names the direct molecular interaction demonstrated by the structure and K307E clamp mutant. Proposed replacements: TPR domain binding Supporting Evidence: PMID:28278223 Yeast Hsp90 C-terminal domain failed to bind the K307E mutant of FKBP92-380 suggesting that its binding was completely disrupted |
| GO:0030911 TPR domain binding | EXP PMID:24012479 High-resolution structural analysis shows how Tah1 tethers H... | ACCEPT | Summary: Tah1 directly tethers yeast Hsp90 to R2TP through a minimal TPR domain that binds the Hsp90 C-terminal peptide. Reason: This is a direct and specific molecular-function annotation: Hsp82 carries a conserved C-terminal MEEVD motif that is recognized by Tah1's TPR domain, providing a structural basis for recruitment of Hsp90 to the R2TP complex. Supporting Evidence: PMID:24012479 Tah1 bridges Hsp90 to R2TP. Its minimal TPR domain includes two TPR motifs and a capping helix |
| GO:0070585 protein localization to mitochondrion | IPI PMID:12526792 Molecular chaperones Hsp90 and Hsp70 deliver preproteins to ... | REMOVE | Summary: The Tom70 mitochondrial-import paper contrasts mammalian Hsp90-dependent import with yeast import that uses Hsp70 rather than Hsp90. Reason: The supporting abstract explicitly states that yeast preprotein import uses Hsp70 rather than Hsp90. This does not support annotating yeast Hsp82 to protein localization to mitochondrion. Supporting Evidence: PMID:12526792 In yeast, Hsp70 rather than Hsp90 is used in import, and Hsp70 docking is required for the formation of a productive preprotein/Tom70 complex |
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Download this section (compressed HTML)Q: Which client proteins (kinases, transcription factors, ribosome assembly factors) most strongly depend on HSP82 nucleotide-state transitions, and how do conformational dwell times map to client maturation efficiency?
Q: How does the HSP82/HSC82 paralog ratio shift the chaperone interactome composition (co-chaperones, clients) under heat versus standard growth, and what fraction of clients are paralog-specific?
Q: What role does single-site phosphorylation (e.g., starvation-dependent) play in compartment-specific HSP82 localization (nucleus vs cytoplasm) and client engagement?
Experiment: Deplete or inhibit HSP82 (e.g., temperature-sensitive alleles, radicicol) and use AP-MS to map condition-dependent client losses, comparing standard growth to heat shock and starvation conditions to dissect core vs. stress-specific clientele.
Experiment: Reconstitute the full Hsp82 conformational cycle in vitro with purified HSP82 dimers, ATP, and a panel of co-chaperones (Sti1, Aha1, Sba1, Cdc37, Cpr6/7, Cns1) plus a model client kinase, and use single-molecule FRET to measure ATP-dependent open/closed dwell times.
Experiment: Generate separation-of-function HSP82 alleles that selectively impair ATPase, dimerization, or co-chaperone binding (using systematic mutagenesis of the M-domain) and measure client-specific phenotypes (e.g., HAP1, telomerase, R2TP, proteasome) to dissect contributions to each downstream pathway.
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Download this section (compressed HTML)Hsp90 chaperone; functionally redundant with Hsc82p; required for pheromone signaling; negative regulator of the Hsf1p-dependent heat shock response with Cpr7p; docks with Tom70p for mitochondrial preprotein delivery; promotes telomerase DNA binding, nucleotide addition; promotes solubility of chaperone-substrate complexes; DNA damage induced nuclear import is Aha1p dependent; protein abundance increases in response to DNA replication stress; human homolog, HSP90AB1, complements null mutant
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