BAIT
HSP104
chaperone ATPase HSP104, L000000823, YLL026W
Disaggregase; heat shock protein that cooperates with Ydj1p (Hsp40) and Ssa1p (Hsp70) to refold and reactivate previously denatured, aggregated proteins; responsive to stresses including: heat, ethanol, and sodium arsenite; involved in [PSI+] propagation; protein becomes more abundant and forms cytoplasmic foci in response to DNA replication stress; potentiated Hsp104p variants decrease TDP-43 proteotoxicity by eliminating its cytoplasmic aggregation
GO Process (7)
GO Function (5)
GO Component (3)
Gene Ontology Biological Process
- cellular heat acclimation [IMP]
- chaperone cofactor-dependent protein refolding [IDA]
- inheritance of oxidatively modified proteins involved in replicative cell aging [IGI, IMP]
- protein folding in endoplasmic reticulum [IMP]
- protein unfolding [IMP]
- stress granule disassembly [IDA]
- trehalose metabolism in response to heat stress [IMP]
Gene Ontology Molecular Function
Saccharomyces cerevisiae (S288c)
PREY
HOF1
CYK2, formin-binding protein HOF1, L000004406, YMR032W
SH3 domain-containing protein required for cytokinesis; localized to bud neck; phosphorylated by Dbf2p; regulates actomyosin ring dynamics and septin localization; interacts with the formins, Bni1p and Bnr1p, and with Cyk3p, Vrp1p, and Bni5p
GO Process (3)
GO Function (1)
GO Component (3)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Saccharomyces cerevisiae (S288c)
Synthetic Lethality
A genetic interaction is inferred when mutations or deletions in separate genes, each of which alone causes a minimal phenotype, result in lethality when combined in the same cell under a given condition.
Publication
The yeast AAA+ chaperone Hsp104 is part of a network that links the actin cytoskeleton with the inheritance of damaged proteins.
The yeast AAA(+) chaperone Hsp104 is essential for the development of thermotolerance and for the inheritance of prions. Recently, Hsp104, together with the actin cytoskeleton, has been implicated in the asymmetric distribution of carbonylated proteins. Here, we investigated the interplay between Hsp104 and actin by using a dominant-negative variant of Hsp104 (HAP/ClpP) that degrades substrate proteins instead of remodeling them. ... [more]
Mol. Cell. Biol. Jul. 01, 2009; 29(13);3738-45 [Pubmed: 19398583]
Throughput
- Low Throughput
Ontology Terms
- phenotype: heat sensitivity (APO:0000147)
- phenotype: inviable (APO:0000112)
Curated By
- BioGRID