Critical role for a central part of Mdm2 in the ubiquitylation of p53.

@article{Meulmeester2003CriticalRF,
  title={Critical role for a central part of Mdm2 in the ubiquitylation of p53.},
  author={Erik Meulmeester and Ruth Frenk and Robert Stad and Petra de Graaf and Jean-Christophe Marine and Karen H Vousden and Aart Jochemsen},
  journal={Molecular and cellular biology},
  year={2003},
  volume={23 14},
  pages={
          4929-38
        }
}
The stability of the p53 protein is regulated by Mdm2. By acting as an E3 ubiquitin ligase, Mdm2 directs the ubiquitylation of p53 and its subsequent degradation by the 26S proteasome. In contrast, the Mdmx protein, although structurally similar to Mdm2, cannot ubiquitylate or degrade p53 in vivo. To ascertain which domains determine this functional difference between Mdm2 and Mdmx and consequently are essential for p53 ubiquitylation and degradation, we generated Mdm2-Mdmx chimeric constructs… CONTINUE READING

Topics from this paper.

Citations

Publications citing this paper.
SHOWING 1-10 OF 56 CITATIONS, ESTIMATED 71% COVERAGE

Signaling to p53: ribosomal proteins find their way.

  • Cancer cell
  • 2009
VIEW 21 EXCERPTS
CITES RESULTS & BACKGROUND
HIGHLY INFLUENCED

Modulation of p53 degradation via MDM2-mediated ubiquitylation and the ubiquitin-proteasome system during reperfusion after stroke: role of oxidative stress.

  • Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism
  • 2005
VIEW 1 EXCERPT
CITES BACKGROUND
HIGHLY INFLUENCED

Regulation of the MDM2-p53 feedback loop by ribosomal proteins

VIEW 4 EXCERPTS
CITES BACKGROUND
HIGHLY INFLUENCED

FILTER CITATIONS BY YEAR

2005
2019

CITATION STATISTICS

  • 3 Highly Influenced Citations