BAIT

VAM6

CVT4, VPL18, VPL22, VPS39, L000003935, YDL077C
Subunit of the HOPS endocytic tethering complex; vacuole membrane protein that functions as a Rab GTPase effector, interacting with both GTP- and GDP-bound conformations of Ypt7p, facilitating tethering and promoting several membrane fusion events at the late endosome and vacuole; required for both membrane and protein trafficking
Saccharomyces cerevisiae (S288c)
PREY

NCS6

TUC1, YGL210W-A, YGL211W
Protein required for uridine thiolation of Gln, Lys, and Glu tRNAs; required for the thiolation of uridine at the wobble position of Gln, Lys, and Glu tRNAs; has a role in urmylation and in invasive and pseudohyphal growth; inhibits replication of Brome mosaic virus in S. cerevisiae
GO Process (3)
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

A dynamic interface between vacuoles and mitochondria in yeast.

Elbaz-Alon Y, Rosenfeld-Gur E, Shinder V, Futerman AH, Geiger T, Schuldiner M

Cellular life depends on continuous transport of lipids and small molecules between mitochondria and the endomembrane system. Recently, endoplasmic reticulum-mitochondrial encounter structure (ERMES) was identified as an important yet nonessential contact for such transport. Using a high-content screen in yeast, we found a contact site, marked by Vam6/Vps39, between vacuoles (the yeast lysosomal compartment) and mitochondria, named vCLAMP (vacuole and mitochondria patch). ... [more]

Dev. Cell Jul. 14, 2014; 30(1);95-102 [Pubmed: 25026036]

Throughput

  • High Throughput

Additional Notes

  • Table S2

Curated By

  • BioGRID