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

The TRIM4 E3 ubiquitin ligase degrades TPL2 and is modulated by oncogenic KRAS.

Bansod S, Dodhiawala PB, Geng Y, Bulle A, Liu P, Li L, Townsend R, Grierson PM, Held JM, Adhikari H, Lim KH

Loss-of-function mutations in the C terminus of TPL2 kinase promote oncogenesis by impeding its proteasomal degradation, leading to sustained protein expression. However, the degradation mechanism for TPL2 has remained elusive. Through proximity-dependent biotin identification (BioID), we uncovered tripartite motif-containing 4 (TRIM4) as the E3 ligase that binds and degrades TPL2 by polyubiquitination of lysines 415 and 439. The naturally occurring ... [more]

Cell Rep Sep. 24, 2024; 43(9);114667 [Pubmed: 39178114]

Throughput

  • High Throughput

Additional Notes

  • Affinity capture MS was carried out to identify high confidence protein interactors of mutant KRAS-G12V with greater than 10 matched sequences and enriched by greater than or equal to 3 fold over control

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
KRAS RAB11FIP5
Proximity Label-MS
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.

High14.41BioGRID
2991716

Curated By

  • BioGRID