Back to your heart: ubiquitin proteasome system-regulated signal transduction

J Mol Cell Cardiol. 2012 Mar;52(3):526-37. doi: 10.1016/j.yjmcc.2011.10.023. Epub 2011 Nov 6.

Abstract

Awareness of the regulation of cell signaling by post-translational ubiquitination has emerged over the past 2 decades. Like phosphorylation, post-translational modification of proteins with ubiquitin can result in the regulation of numerous cellular functions, for example, the DNA damage response, apoptosis, cell growth, and the innate immune response. In this review, we discuss recently published mechanisms by which the ubiquitin proteasome system regulates key signal transduction pathways in the heart, including MAPK JNK, calcineurin, FOXO, p53, and estrogen receptors α and β. We then explore how ubiquitin proteasome system-specific regulation of these signal transduction pathways plays a role in the pathophysiology of common cardiac diseases, such as cardiac hypertrophy, heart failure, ischemia reperfusion injury, and diabetes. This article is part of a Special Section entitled "Post-translational Modification."

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Animals
  • Calcineurin / metabolism
  • Forkhead Transcription Factors / metabolism
  • Heart / physiology
  • Humans
  • MAP Kinase Signaling System
  • Myocardium / metabolism*
  • Proteasome Endopeptidase Complex / metabolism*
  • Receptors, Estrogen / metabolism
  • Signal Transduction*
  • Tumor Suppressor Protein p53 / metabolism
  • Ubiquitin / metabolism*
  • Ubiquitination

Substances

  • Forkhead Transcription Factors
  • Receptors, Estrogen
  • Tumor Suppressor Protein p53
  • Ubiquitin
  • Calcineurin
  • Proteasome Endopeptidase Complex