BAIT

HSP78

chaperone ATPase HSP78, L000000821, YDR258C
Oligomeric mitochondrial matrix chaperone; cooperates with Ssc1p in mitochondrial thermotolerance after heat shock; able to prevent the aggregation of misfolded proteins as well as resolubilize protein aggregates
GO Process (5)
GO Function (2)
GO Component (2)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)
PREY

YIP4

YGL198W
Protein that interacts with Rab GTPases; localized to late Golgi vesicles; computational analysis of large-scale protein-protein interaction data suggests a possible role in vesicle-mediated transport
GO Process (0)
GO Function (1)
GO Component (2)

Gene Ontology Molecular Function

Gene Ontology Cellular Component

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

Distinct types of intramitochondrial protein aggregates protect mitochondria against proteotoxic stress.

Bertgen L, Boekenkamp JE, Schneckmann T, Koch C, Raeschle M, Storchova Z, Herrmann JM

Mitochondria consist of hundreds of proteins, most of which are inaccessible to the proteasomal quality control system of the cytosol. How cells stabilize the mitochondrial proteome during challenging conditions remains poorly understood. Here, we show that mitochondria form spatially defined protein aggregates as a stress-protecting mechanism. Two different types of intramitochondrial protein aggregates can be distinguished. The mitoribosomal protein Var1 ... [more]

Cell Rep Apr. 23, 2024; 43(4);114018 [Pubmed: 38551959]

Throughput

  • High Throughput

Additional Notes

  • in rho0 background

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
YIP4 HSP78
Negative Genetic
Negative Genetic

Mutations/deletions in separate genes, each of which alone causes a minimal phenotype, but when combined in the same cell results in a more severe fitness defect or lethality under a given condition. This term is reserved for high or low throughput studies with scores.

High-0.3841BioGRID
2117963

Curated By

  • BioGRID