SCF-mediated protein degradation and cell cycle control

Xiaolu L. Ang, J. Wade Harper

Research output: Contribution to journalReview article

140 Scopus citations

Abstract

The regulatory step in ubiquitin (Ub)-mediated protein degradation involves recognition and selection of the target substrate by an E3 Ub-ligase. E3 Ub-ligases evoke sophisticated mechanisms to regulate their activity temporally and spatially, including multiple post-translational modifications, combinatorial E3 Ub-ligase pathways, and subcellular localization. The phosphodegrons of many substrates incorporate the activities of multiple kinases, and ubiquitination only occurs when all necessary phosphorylation signals have been incorporated. In this manner, the precise timing of degradation can be controlled. Another way that the Ub pathway tightly controls the timing of proteolysis is with multiple E3 Ub-ligases acting upon a single target. Lastly, subcellular localization can either promote or prevent degradation by regulating the accessibility of kinases and E3 Ub-ligases. This review highlights recent findings that exemplify these emerging themes in the regulation of E3 Ub-ligase substrate recognition.

Original languageEnglish (US)
Pages (from-to)2860-2870
Number of pages11
JournalOncogene
Volume24
Issue number17
DOIs
StatePublished - Apr 18 2005

Keywords

  • APC
  • E3 ubiquitin-ligase
  • Phosphodegron
  • Proteolysis
  • SCF
  • Ubiquitin

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Cancer Research

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