BAIT
HSP82
HSP90, Hsp90 family chaperone HSP82, L000000822, YPL240C
Hsp90 chaperone; redundant in function with Hsc82p; required for pheromone signaling, negative regulation of Hsf1p; docks with Tom70p for mitochondrial preprotein delivery; promotes telomerase DNA binding, nucleotide addition; protein abundance increases in response to DNA replication stress; contains two acid-rich unstructured regions that promote solubility of chaperone-substrate complexes; HSP82 has a paralog, HSC82, that arose from the whole genome duplication
GO Process (7)
GO Function (2)
GO Component (1)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Saccharomyces cerevisiae (S288c)
PREY
PEA2
DFG9, PPF2, L000003143, YER149C
Coiled-coil 12S polarisome subunit; required for polarity establishment, apical bud growth, shmoo formation, filamentous differentiation; involved in Bni1p localization at sites of polarized growth, controlling polarized assembly of actin cables; role in apical growth affects diploid-specific bipolar bud site selection; retains Slt2p at bud tip to regulate ER inheritance; role in Ca2+ influx, cell fusion; S288C allele encoding Leu409 rather than Met linked with non-invasion
GO Process (9)
GO Function (0)
GO Component (6)
Gene Ontology Biological Process
- bipolar cellular bud site selection [IMP]
- budding cell apical bud growth [IGI, IMP]
- establishment of cell polarity [IMP]
- filamentous growth [IMP]
- positive regulation of actin cytoskeleton reorganization [IMP]
- pseudohyphal growth [IMP]
- regulation of initiation of mating projection growth [IMP]
- regulation of protein localization [IMP]
- regulation of termination of mating projection growth [IMP]
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
Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone.
Physical, genetic, and chemical-genetic interactions centered on the conserved chaperone Hsp90 were mapped at high resolution in yeast using systematic proteomic and genomic methods. Physical interactions were identified using genome-wide two hybrid screens combined with large-scale affinity purification of Hsp90-containing protein complexes. Genetic interactions were uncovered using synthetic genetic array technology and by a microarray-based chemical-genetic screen of a set ... [more]
Cell Mar. 11, 2005; 120(5);715-27 [Pubmed: 15766533]
Throughput
- High Throughput
Ontology Terms
- phenotype: inviable (APO:0000112)
Curated By
- BioGRID