A novel p53 phosphorylation site within the MDM2 ubiquitination signal: I. phosphorylation at SER269 in vivo is linked to inactivation of p53 function.

@article{Fraser2010ANP,
  title={A novel p53 phosphorylation site within the MDM2 ubiquitination signal: I. phosphorylation at SER269 in vivo is linked to inactivation of p53 function.},
  author={Jennifer A Fraser and Borivoj Vojtesek and Ted R. Hupp},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 48},
  pages={37762-72}
}
p53 is a thermodynamically unstable protein containing a conformationally flexible multiprotein docking site within the DNA-binding domain. A combinatorial peptide chip used to identify the novel kinase consensus site RXSΦ(K/D) led to the discovery of a homologous phosphorylation site in the S10 β-strand of p53 at Ser(269). Overlapping peptide libraries confirmed that Ser(269) was a phosphoacceptor site in vitro, and immunochemical approaches evaluated whether p53 is phosphorylated in vivo at… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 10 extracted citations

Structural and sequential context of p53: A review of experimental and theoretical evidence.

Progress in biophysics and molecular biology • 2015
View 4 Excerpts
Highly Influenced

Similar Papers

Loading similar papers…