Mutational analysis of Mdm2 C-terminal tail suggests an evolutionarily conserved role of its length in Mdm2 activity toward p53 and indicates structural differences between Mdm2 homodimers and Mdm2/MdmX heterodimers

@article{Doleelov2012MutationalAO,
  title={Mutational analysis of Mdm2 C-terminal tail suggests an evolutionarily conserved role of its length in Mdm2 activity toward p53 and indicates structural differences between Mdm2 homodimers and Mdm2/MdmX heterodimers},
  author={P. Dole{\vz}elov{\'a} and Kateřina Cetkovsk{\'a} and K. Vousden and S. Uldrijan},
  journal={Cell Cycle},
  year={2012},
  volume={11},
  pages={953 - 962}
}
  • P. Doleželová, Kateřina Cetkovská, +1 author S. Uldrijan
  • Published 2012
  • Biology, Medicine
  • Cell Cycle
  • Mdm2 can mediate p53 ubiquitylation and degradation either in the form of the Mdm2 homodimer or Mdm2/MdmX heterodimer. The ubiquitin ligase activity of these complexes resides mainly in their respective RING finger domains and also requires adjacent C-terminal tails. So far, structural studies have failed to show significant differences between Mdm2 RING homodimers and Mdm2/MdmX RING heterodimers. Here, we report that not only the primary amino acid sequence, but also the length of the C… CONTINUE READING
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