PFD1 encodes the Pfd1/Gim6 beta-type subunit of the cytosolic prefoldin complex, an ATP-independent cochaperone that captures nonnative actin and tubulin folding intermediates and delivers them to CCT/TRiC, with secondary nuclear roles in transcription elongation.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0006457 protein folding | IBA GO_REF:0000033 | ACCEPT | Summary: protein folding reviewed for PFD1: ACCEPT. Reason: Retain as the direct biological process served by Pfd1-containing prefoldin in cytosolic actin/tubulin folding. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN002325135 SUPPORTS TRANSFER Current PTHR20903 PAINT retains protein folding at this prefoldin beta-family node, with target SGD:S000003715 among experimentally grounded descendants. Supporting Evidence: PMID:9630229 Prefoldin binds specifically to cytosolic chaperonin (c-cpn) and transfers target proteins to it |
| GO:0051082 unfolded protein binding | IBA GO_REF:0000033 | MODIFY | Summary: unfolded protein binding reviewed for PFD1: MODIFY. Reason: Unfolded protein binding is mechanistically close but too broad; Pfd1 is best represented as a prefoldin protein-folding cochaperone, and current PTHR20903 PAINT has already moved this node from GO:0051082 to GO:0044183. Propagation Review Root cause: SOURCE STALE OR MISSING Sources checked: PANTHER:PTN002325135 SOURCE STALE OR MISSING GO:0051082 no longer appears as an IBD on the current PTHR20903 PAINT node; the same node now carries GO:0044183, matching the project-wide prefoldin replacement. Proposed replacements: protein folding chaperone Supporting Evidence: file:yeast/PFD1/PFD1-deep-research-falcon.md prefoldin functions largely as an **ATP-independent holdase**, stabilizing folding intermediates and preventing aggregation prior to transfer to CCT/TRiC |
| GO:0005737 cytoplasm | IBA GO_REF:0000033 | ACCEPT | Summary: cytoplasm reviewed for PFD1: ACCEPT. Reason: Retain as the principal cellular compartment for the canonical prefoldin to CCT/TRiC folding pathway. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN002325135 SUPPORTS TRANSFER Current PTHR20903 PAINT retains cytoplasm at this prefoldin beta-family node, and cytoplasmic TRiC handoff is the canonical prefoldin context. Supporting Evidence: file:yeast/PFD1/PFD1-deep-research-falcon.md The central pathway involving Pfd1 is the **cytosolic folding pipeline** for cytoskeletal proteins |
| GO:0044183 protein folding chaperone | IBA GO_REF:0000033 | ACCEPT | Summary: protein folding chaperone reviewed for PFD1: ACCEPT. Reason: Retain as the best molecular-function term for the ATP-independent prefoldin cochaperone role. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN002325135 SUPPORTS TRANSFER Current PTHR20903 PAINT carries GO:0044183 at this ancestral node; it is the appropriate functional term for conserved prefoldin-assisted substrate transfer to CCT/TRiC. Supporting Evidence: PMID:9630229 Prefoldin binds specifically to cytosolic chaperonin (c-cpn) and transfers target proteins to it |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: cytoplasm reviewed for PFD1: ACCEPT. Reason: Retain as the principal cellular compartment for the canonical prefoldin to CCT/TRiC folding pathway. Supporting Evidence: file:yeast/PFD1/PFD1-deep-research-falcon.md The central pathway involving Pfd1 is the **cytosolic folding pipeline** for cytoskeletal proteins |
| GO:0006457 protein folding | IEA GO_REF:0000002 | ACCEPT | Summary: protein folding reviewed for PFD1: ACCEPT. Reason: Retain as the direct biological process served by Pfd1-containing prefoldin in cytosolic actin/tubulin folding. Supporting Evidence: PMID:9630229 Prefoldin binds specifically to cytosolic chaperonin (c-cpn) and transfers target proteins to it |
| GO:0016272 prefoldin complex | IEA GO_REF:0000002 | ACCEPT | Summary: prefoldin complex reviewed for PFD1: ACCEPT. Reason: Retain; Pfd1/Gim6 is a component of the heterohexameric prefoldin complex. Supporting Evidence: PMID:9630229 discovery of a heterohexameric chaperone protein, prefoldin |
| GO:0051082 unfolded protein binding | IEA GO_REF:0000002 | MODIFY | Summary: unfolded protein binding reviewed for PFD1: MODIFY. Reason: Unfolded protein binding is mechanistically close but too broad; Pfd1 is best represented as a prefoldin protein-folding cochaperone. Proposed replacements: protein folding chaperone Supporting Evidence: file:yeast/PFD1/PFD1-deep-research-falcon.md prefoldin functions largely as an **ATP-independent holdase**, stabilizing folding intermediates and preventing aggregation prior to transfer to CCT/TRiC |
| GO:0005515 protein binding | IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine... | REMOVE | Summary: protein binding reviewed for PFD1: REMOVE. Reason: Remove the generic molecular-function row, not the underlying interaction evidence. Protein binding is too uninformative as a standalone assertion for Pfd1; prefoldin complex membership and chaperone activity capture the functional interaction context. Supporting Evidence: file:yeast/PFD1/PFD1-deep-research-falcon.md prefoldin binds client proteins via the distal regions ("tentacle tips") and/or the cavity of the hexamer |
| GO:0005515 protein binding | IPI PMID:16554755 Global landscape of protein complexes in the yeast Saccharom... | REMOVE | Summary: protein binding reviewed for PFD1: REMOVE. Reason: Remove the generic molecular-function row, not the underlying interaction evidence. Protein binding is too uninformative as a standalone assertion for Pfd1; prefoldin complex membership and chaperone activity capture the functional interaction context. Supporting Evidence: file:yeast/PFD1/PFD1-deep-research-falcon.md prefoldin binds client proteins via the distal regions ("tentacle tips") and/or the cavity of the hexamer |
| GO:0005515 protein binding | IPI PMID:19536198 An atlas of chaperone-protein interactions in Saccharomyces ... | REMOVE | Summary: protein binding reviewed for PFD1: REMOVE. Reason: Remove the generic molecular-function row, not the underlying interaction evidence. Protein binding is too uninformative as a standalone assertion for Pfd1; prefoldin complex membership and chaperone activity capture the functional interaction context. Supporting Evidence: file:yeast/PFD1/PFD1-deep-research-falcon.md prefoldin binds client proteins via the distal regions ("tentacle tips") and/or the cavity of the hexamer |
| GO:0005515 protein binding | IPI PMID:37968396 The social and structural architecture of the yeast protein ... | REMOVE | Summary: protein binding reviewed for PFD1: REMOVE. Reason: Remove the generic molecular-function row, not the underlying interaction evidence. Protein binding is too uninformative as a standalone assertion for Pfd1; prefoldin complex membership and chaperone activity capture the functional interaction context. Supporting Evidence: file:yeast/PFD1/PFD1-deep-research-falcon.md prefoldin binds client proteins via the distal regions ("tentacle tips") and/or the cavity of the hexamer |
| GO:0005515 protein binding | IPI PMID:9878052 Compartmentation of protein folding in vivo: sequestration o... | REMOVE | Summary: protein binding reviewed for PFD1: REMOVE. Reason: Remove the generic molecular-function row, not the underlying interaction evidence. Protein binding is too uninformative as a standalone assertion for Pfd1; prefoldin complex membership and chaperone activity capture the functional interaction context. Supporting Evidence: file:yeast/PFD1/PFD1-deep-research-falcon.md prefoldin binds client proteins via the distal regions ("tentacle tips") and/or the cavity of the hexamer |
| GO:0006457 protein folding | NAS PMID:9463374 A novel protein complex promoting formation of functional al... | ACCEPT | Summary: protein folding reviewed for PFD1: ACCEPT. Reason: Retain as the direct biological process served by Pfd1-containing prefoldin in cytosolic actin/tubulin folding. Supporting Evidence: PMID:9463374 protein complex that promotes formation of functional alpha- and gamma-tubulin |
| GO:0032968 positive regulation of transcription elongation by RNA polymerase II | IMP PMID:24068951 The prefoldin complex regulates chromatin dynamics during tr... | KEEP AS NON CORE | Summary: positive regulation of transcription elongation by RNA polymerase II reviewed for PFD1: KEEP_AS_NON_CORE. Reason: Keep as an evidence-supported secondary nuclear/chromatin role, but do not treat it as the core evolved role of Pfd1. Supporting Evidence: PMID:24068951 establishes the involvement of prefoldin in transcription elongation |
| GO:0032968 positive regulation of transcription elongation by RNA polymerase II | IGI PMID:24068951 The prefoldin complex regulates chromatin dynamics during tr... | KEEP AS NON CORE | Summary: positive regulation of transcription elongation by RNA polymerase II reviewed for PFD1: KEEP_AS_NON_CORE. Reason: Keep as an evidence-supported secondary nuclear/chromatin role, but do not treat it as the core evolved role of Pfd1. Supporting Evidence: PMID:24068951 establishes the involvement of prefoldin in transcription elongation |
| GO:0006457 protein folding | IMP PMID:9630229 Prefoldin, a chaperone that delivers unfolded proteins to cy... | ACCEPT | Summary: protein folding reviewed for PFD1: ACCEPT. Reason: Retain as the direct biological process served by Pfd1-containing prefoldin in cytosolic actin/tubulin folding. Supporting Evidence: PMID:9878052 GimC accelerates actin folding at least 5-fold and prevents the premature release of non-native protein from TRiC |
| GO:0007010 cytoskeleton organization | IMP PMID:9630229 Prefoldin, a chaperone that delivers unfolded proteins to cy... | KEEP AS NON CORE | Summary: cytoskeleton organization reviewed for PFD1: KEEP_AS_NON_CORE. Reason: Keep as a downstream consequence of actin/tubulin folding defects rather than the direct molecular role. Supporting Evidence: PMID:9630229 impaired functions of the actin and tubulin-based cytoskeleton |
| GO:0016272 prefoldin complex | IMP PMID:9630229 Prefoldin, a chaperone that delivers unfolded proteins to cy... | ACCEPT | Summary: prefoldin complex reviewed for PFD1: ACCEPT. Reason: Retain; Pfd1/Gim6 is a component of the heterohexameric prefoldin complex. Supporting Evidence: PMID:9630229 discovery of a heterohexameric chaperone protein, prefoldin |
| GO:0051082 unfolded protein binding | IMP PMID:9630229 Prefoldin, a chaperone that delivers unfolded proteins to cy... | MODIFY | Summary: unfolded protein binding reviewed for PFD1: MODIFY. Reason: Unfolded protein binding is mechanistically close but too broad; Pfd1 is best represented as a prefoldin protein-folding cochaperone. Proposed replacements: protein folding chaperone Supporting Evidence: file:yeast/PFD1/PFD1-deep-research-falcon.md prefoldin functions largely as an **ATP-independent holdase**, stabilizing folding intermediates and preventing aggregation prior to transfer to CCT/TRiC |
| GO:0016272 prefoldin complex | IPI PMID:9463374 A novel protein complex promoting formation of functional al... | ACCEPT | Summary: Pfd1/Gim6 is a core subunit of the heterohexameric prefoldin/GimC complex. Reason: Accept the new ComplexPortal part_of assertion. The local PMID:9463374 cache is abstract-only, but the original Gim complex paper established a common cytoplasmic Gim complex and later prefoldin work established the heterohexameric complex containing Pfd1/Gim6; this row is biologically correct and agrees with the InterPro prefoldin-complex row. Supporting Evidence: PMID:9463374 cytoplasmic Gim proteins encoded by these GIM genes are present in common complexes PMID:9630229 discovery of a heterohexameric chaperone protein, prefoldin |
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Download this section (compressed HTML)Q: Which Pfd1-containing prefoldin surfaces distinguish cytoskeletal client capture from the secondary nuclear transcription role?
Q: Does Pfd1 have subunit-specific client preferences within yeast prefoldin beyond the canonical actin and tubulin pathway?
Experiment: Generate Pfd1 separation-of-function mutants at endogenous expression levels and compare actin/tubulin folding, prefoldin complex integrity, chromatin occupancy, and RNA polymerase II elongation phenotypes.
Hypothesis: Pfd1 has separable surfaces for canonical actin/tubulin cochaperone function and non-core transcription-associated function.
Type: separation-of-function mutagenesis
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Download this section (compressed HTML)Subunit of heterohexameric prefoldin; prefoldin binds cytosolic chaperonin and transfers target proteins to it; involved in the biogenesis of actin and of alpha- and gamma-tubulin; prefoldin complex also localizes to chromatin of actively transcribed genes in the nucleus and facilitates transcriptional elongation
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