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 RPL22
Affinity Capture-MS
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.

High-BioGRID
-
KRAS RPL22
Synthetic Lethality
Synthetic Lethality

A genetic interaction is inferred when mutations or deletions in separate genes, each of which alone causes a minimal phenotype, result in lethality when combined in the same cell under a given condition.

High-BioGRID
2619370

Curated By

  • BioGRID