VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases.

@article{Kamura2004VHLboxAS,
  title={VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases.},
  author={Takumi Kamura and Katsumi Maenaka and Shuhei Kotoshiba and Mitsuyuki Matsumoto and Daisuke Kohda and Ronald C. Conaway and Joan W Conaway and Keiichi I Nakayama},
  journal={Genes & development},
  year={2004},
  volume={18 24},
  pages={
          3055-65
        }
}
The ECS (Elongin B/C-Cul2/Cul5-SOCS-box protein) complex is a member of a family of ubiquitin ligases that share a Cullin-Rbx module. SOCS-box proteins recruit substrates to the ECS complex and are linked to Cullin-Rbx via Elongin B/C. VHL has been implicated as a SOCS-box protein, but lacks a C-terminal sequence (downstream of the BC box) of the SOCS box. We now show that VHL specifically interacts with endogenous Cul2-Rbx1 in mammalian cells, whereas SOCS-box proteins associate with Cul5-Rbx2… CONTINUE READING
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