Two-hybrid

Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.

Publication

Cbl interacts with multiple E2s in vitro and in cells.

Liyasova MS, Ma K, Voeller D, Ryan PE, Chen J, Klevit RE, Lipkowitz S

Many receptor tyrosine kinases (RTKs, such as EGFR, MET) are negatively regulated by ubiquitination and degradation mediated by Cbl proteins, a family of RING finger (RF) ubiquitin ligases (E3s). Loss of Cbl protein function is associated with malignant transformation driven by increased RTK activity. RF E3s, such as the Cbl proteins, interact with a ubiquitin-conjugating enzyme (E2) to confer specificity ... [more]

PLoS ONE May. 24, 2019; 14(5);e0216967 [Pubmed: 31120930]

Throughput

  • Low Throughput

Additional Notes

  • The activated Cbl (Y371E) mutant was used in the yeast two-hybrid screen to capture transient or low affinity interactions.

Curated By

  • BioGRID