The Colossus of ubiquitylation: decrypting a cellular code

Mol Cell. 2013 Feb 21;49(4):591-600. doi: 10.1016/j.molcel.2013.01.028.

Abstract

Ubiquitylation is an essential posttranslational modification that can regulate the stability, activity, and localization of thousands of proteins. The reversible attachment of ubiquitin as well as interpretation of the ubiquitin signal depends on dynamic protein networks that are challenging to analyze. In this perspective, we discuss tools of the trade that have recently been developed to dissect mechanisms of ubiquitin-dependent signaling, thereby revealing the critical features of an important cellular code.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Humans
  • Protein Processing, Post-Translational
  • Protein Stability
  • Proteolysis
  • Signal Transduction
  • Ubiquitin-Protein Ligases / physiology
  • Ubiquitinated Proteins / metabolism*
  • Ubiquitination*

Substances

  • Ubiquitinated Proteins
  • Ubiquitin-Protein Ligases