VprBP binds full-length RAG1 and is required for B-cell development and V(D)J recombination fidelity.

@article{Kassmeier2012VprBPBF,
  title={VprBP binds full-length RAG1 and is required for B-cell development and V(D)J recombination fidelity.},
  author={Michele D. Kassmeier and Koushik Kr. Mondal and Victoria L. Palmer and Prafulla Raval and Sushil Kumar and Greg A. Perry and D. Karl Anderson and Pawel Ciborowski and Sarah Jackson and Yue Xiong and Patrick C. Swanson},
  journal={The EMBO journal},
  year={2012},
  volume={31 4},
  pages={945-58}
}
The N-terminus of full-length RAG1, though dispensable for RAG1/2 cleavage activity, is required for efficient V(D)J recombination. This region supports RING E3 ubiquitin ligase activity in vitro, but whether full-length RAG1 functions as a single subunit or a multi-subunit E3 ligase in vivo is unclear. We show the multi-subunit cullin RING E3 ligase complex VprBP/DDB1/Cul4A/Roc1 associates with full-length RAG1 through VprBP. This complex is assembled into RAG protein-DNA complexes, and… CONTINUE READING