BAIT
CLPP
DFNB81, PRLTS3
caseinolytic mitochondrial matrix peptidase proteolytic subunit
GO Process (1)
GO Function (3)
GO Component (3)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
DHRS4
CR, NRDR, PHCR, PSCD, SCAD-SRL, SDR-SRL, SDR25C1, SDR25C2, UNQ851/PRO1800
dehydrogenase/reductase (SDR family) member 4
GO Process (5)
GO Function (5)
GO Component (7)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
Proximity Label-MS
An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods.
Publication
Mitochondrial ClpP-Mediated Proteolysis Induces Selective Cancer Cell Lethality.
The mitochondrial caseinolytic protease P (ClpP) plays a central role in mitochondrial protein quality control by degrading misfolded proteins. Using genetic and chemical approaches, we showed that hyperactivation of the protease selectively kills cancer cells, independently of p53 status, by selective degradation of its respiratory chain protein substrates and disrupts mitochondrial structure and function, while it does not affect non-malignant cells. We identified ... [more]
Cancer Cell Dec. 13, 2018; 35(5);721-737.e9 [Pubmed: 31056398]
Throughput
- High Throughput
Curated By
- BioGRID