BAIT

HSC82

HSP90, Hsp90 family chaperone HSC82, L000000813, YMR186W
Cytoplasmic chaperone of the Hsp90 family; plays a role in determining prion variants; redundant in function and nearly identical with Hsp82p, and together they are essential; expressed constitutively at 10-fold higher basal levels than HSP82 and induced 2-3 fold by heat shock; contains two acid-rich unstructured regions that promote the solubility of chaperone-substrate complexes; HSC82 has a paralog, HSP82, that arose from the whole genome duplication
Saccharomyces cerevisiae (S288c)
PREY

HSC82

HSP90, Hsp90 family chaperone HSC82, L000000813, YMR186W
Cytoplasmic chaperone of the Hsp90 family; plays a role in determining prion variants; redundant in function and nearly identical with Hsp82p, and together they are essential; expressed constitutively at 10-fold higher basal levels than HSP82 and induced 2-3 fold by heat shock; contains two acid-rich unstructured regions that promote the solubility of chaperone-substrate complexes; HSC82 has a paralog, HSP82, that arose from the whole genome duplication
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

The Hsp90 molecular chaperone governs client proteins by targeting intrinsically disordered regions.

Kolhe JA, Babu NL, Freeman BC

Molecular chaperones govern proteome health to support cell homeostasis. An essential eukaryotic component of the chaperone system is Hsp90. Using a chemical-biology approach, we characterized the features driving the Hsp90 physical interactome. We found that Hsp90 associated with ?20% of the yeast proteome using its three domains to preferentially target intrinsically disordered regions (IDRs) of client proteins. Hsp90 selectively utilized ... [more]

Mol Cell Jun. 15, 2023; 83(12);2035-2044.e7 [Pubmed: 37295430]

Throughput

  • High Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
HSC82 HSC82
Co-crystal Structure
Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Low-BioGRID
-
HSC82 HSC82
FRET
FRET

An interaction is inferred when close proximity of interaction partners is detected by fluorescence resonance energy transfer between pairs of fluorophore-labeled molecules, such as occurs between CFP (donor) and YFP (acceptor) fusion proteins.

Low-BioGRID
-
HSC82 HSC82
Protein-peptide
Protein-peptide

An interaction is detected between a protein and a peptide derived from an interaction partner. This includes phage display experiments.

Low-BioGRID
-
HSC82 HSC82
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
-
HSC82 HSC82
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
3016643

Curated By

  • BioGRID