Ubiquitin-Activated Interaction Traps (UBAITs) identify E3 ligase binding partners.

@article{OConnor2015UbiquitinActivatedIT,
  title={Ubiquitin-Activated Interaction Traps (UBAITs) identify E3 ligase binding partners.},
  author={Hazel F O'Connor and Nancy Lyon and Justin Wai-chung Leung and Poonam Agarwal and Caleb D Swaim and Kyle M Miller and Jon M. Huibregtse},
  journal={EMBO reports},
  year={2015},
  volume={16 12},
  pages={1699-712}
}
We describe a new class of reagents for identifying substrates, adaptors, and regulators of HECT and RING E3s. UBAITs (Ubiquitin-Activated Interaction Traps) are E3-ubiquitin fusion proteins and, in an E1- and E2-dependent manner, the C-terminal ubiquitin moiety forms an amide linkage to proteins that interact with the E3, enabling covalent co-purification of the E3 with partner proteins. We designed UBAITs for both HECT (Rsp5, Itch) and RING (Psh1, RNF126, RNF168) E3s. For HECT E3s, trapping… CONTINUE READING
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