BAIT

GOS1

L000004085, YHL031C
v-SNARE protein involved in Golgi transport; homolog of the mammalian protein GOS-28/GS28
GO Process (2)
GO Function (1)
GO Component (3)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)
PREY

RPL12B

ribosomal 60S subunit protein L12B, L11, YL23, L15B, L12B, L000001711, YDR418W
Ribosomal 60S subunit protein L12B; rpl12a rpl12b double mutant exhibits slow growth and slow translation; homologous to mammalian ribosomal protein L12 and bacterial L11; RPL12B has a paralog, RPL12A, that arose from the whole genome duplication
GO Process (2)
GO Function (1)
GO Component (2)

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

Ubiquitination drives COPI priming and Golgi SNARE localization.

Date SS, Xu P, Hepowit NL, Diab NS, Best J, Xie B, Du J, Strieter ER, Jackson LP, MacGurn JA, Graham TR

Deciphering mechanisms controlling SNARE localization within the Golgi complex is crucial to understanding protein trafficking patterns within the secretory pathway. SNAREs are also thought to prime coatomer protein I (COPI) assembly to ensure incorporation of these essential cargoes into vesicles, but the regulation of these events is poorly understood. Here, we report roles for ubiquitin recognition by COPI in SNARE ... [more]

Elife Jul. 29, 2022; 11(); [Pubmed: 35904239]

Throughput

  • High Throughput

Curated By

  • BioGRID