BAIT

CSM4

YPL200W
Protein required for accurate chromosome segregation during meiosis; involved in meiotic telomere clustering (bouquet formation) and telomere-led rapid prophase movements; functions with meiosis-specific telomere-binding protein Ndj1p; CSM4 has a paralog, MPS2, that arose from the whole genome duplication
Saccharomyces cerevisiae (S288c)
PREY

GET3

ARR4, guanine nucleotide exchange factor GET3, YDL100C
Guanine nucleotide exchange factor for Gpa1p; amplifies G protein signaling; functions as a chaperone under ATP-depleted oxidative stress conditions; subunit of the GET complex, which is involved in ATP dependent Golgi to ER trafficking and insertion of tail-anchored (TA) proteins into the ER membrane under non-stress conditions; has low-level ATPase activity; protein abundance increases in response to DNA replication stress
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

Mps2 links Csm4 and Mps3 to form a telomere-associated LINC complex in budding yeast.

Fan J, Jin H, Koch BA, Yu HG

The linker of the nucleoskeleton and cytoskeleton (LINC) complex is composed of two transmembrane proteins: the KASH domain protein localized to the outer nuclear membrane and the SUN domain protein to the inner nuclear membrane. In budding yeast, the sole SUN domain protein, Mps3, is thought to pair with either Csm4 or Mps2, two KASH-like proteins, to form two separate ... [more]

Life Sci Alliance Dec. 01, 2019; 3(12); [Pubmed: 32967926]

Throughput

  • Low Throughput

Curated By

  • BioGRID