Hetero-oligomerization with MdmX rescues the ubiquitin/Nedd8 ligase activity of RING finger mutants of Mdm2.

@article{Singh2007HeterooligomerizationWM,
  title={Hetero-oligomerization with MdmX rescues the ubiquitin/Nedd8 ligase activity of RING finger mutants of Mdm2.},
  author={Rajesh K. Singh and Saravanakumar Iyappan and Martin Scheffner},
  journal={The Journal of biological chemistry},
  year={2007},
  volume={282 15},
  pages={10901-7}
}
Mdm2 is a member of the RING finger family of ubiquitin ligases and is best known for its role in targeting the tumor suppressor p53 for ubiquitination and degradation. Mdm2 can bind to itself and to the structurally related protein MdmX, and these interactions involve the RING finger domain of Mdm2 and MdmX, respectively. In this study, we performed a mutational analysis of the RING finger domain of Mdm2, and we identified several amino acid residues that are important for Mdm2 to exert its… CONTINUE READING