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
Synthetic Protein Interaction Project
Saccharomyces cerevisiae (S288c)
PREY

SNF1

CAT1, CCR1, GLC2, HAF3, PAS14, AMP-activated serine/threonine-protein kinase catalytic subunit SNF1, L000001944, YDR477W
AMP-activated serine/threonine protein kinase; found in a complex containing Snf4p and members of the Sip1p/Sip2p/Gal83p family; required for transcription of glucose-repressed genes, thermotolerance, sporulation, and peroxisome biogenesis; involved in regulation of the nucleocytoplasmic shuttling of Hxk2p; regulates filamentous growth in response to starvation; SUMOylation by Mms21p inhibits its function and targets Snf1p for destruction via the Slx5-Slx8 Ubiquitin ligase
Kinome Project (Sc)
UPS Project
Saccharomyces cerevisiae (S288c)

Affinity Capture-MS

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.

Publication

Mps1 Mediated Phosphorylation of Hsp90 Confers Renal Cell Carcinoma Sensitivity and Selectivity to Hsp90 Inhibitors.

Woodford MR, Truman AW, Dunn DM, Jensen SM, Cotran R, Bullard R, Abouelleil M, Beebe K, Wolfgeher D, Wierzbicki S, Post DE, Caza T, Tsutsumi S, Panaretou B, Kron SJ, Trepel JB, Landas S, Prodromou C, Shapiro O, Stetler-Stevenson WG, Bourboulia D, Neckers L, Bratslavsky G, Mollapour M

The molecular chaperone Hsp90 protects deregulated signaling proteins that are vital for tumor growth and survival. Tumors generally display sensitivity and selectivity toward Hsp90 inhibitors; however, the molecular mechanism underlying this phenotype remains undefined. We report that the mitotic checkpoint kinase Mps1 phosphorylates a conserved threonine residue in the amino-domain of Hsp90. This, in turn, regulates chaperone function by reducing ... [more]

Cell Rep Feb. 02, 2016; 14(4);872-84 [Pubmed: 26804907]

Throughput

  • High Throughput

Additional Notes

  • Table S2

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
HSP82 SNF1
Synthetic Lethality
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.

High-BioGRID
166979

Curated By

  • BioGRID