BAIT
APJ1
YNL077W
Chaperone with a role in SUMO-mediated protein degradation; member of the DnaJ-like family; conserved across eukaryotes; overexpression interferes with propagation of the [Psi+] prion; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies; forms nuclear foci upon DNA replication stress
GO Process (1)
GO Function (2)
GO Component (3)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Saccharomyces cerevisiae (S288c)
PREY
LSM4
SDB23, USS1, L000002447, YER112W
Lsm (Like Sm) protein; part of heteroheptameric complexes (Lsm2p-7p and either Lsm1p or 8p): cytoplasmic Lsm1p complex involved in mRNA decay; nuclear Lsm8p complex part of U6 snRNP and possibly involved in processing tRNA, snoRNA, and rRNA; forms cytoplasmic foci upon DNA replication stress
GO Process (3)
GO Function (1)
GO Component (7)
Gene Ontology Biological Process
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
Chaperone-Mediated Protein Disaggregation Triggers Proteolytic Clearance of Intra-nuclear Protein Inclusions.
The formation of insoluble inclusions in the cytosol and nucleus is associated with impaired protein homeostasis and is a hallmark of several neurodegenerative diseases. Due to the absence of the autophagic machinery, nuclear protein aggregates require a solubilization step preceding degradation by the 26S proteasome. Using yeast, we identify a nuclear protein quality control pathway required for the clearance of ... [more]
Cell Rep Dec. 02, 2019; 31(9);107680 [Pubmed: 32492414]
Throughput
- High Throughput
Additional Notes
- interaction detected after heat shock
Curated By
- BioGRID