| Literature DB >> 22085703 |
Andrea L Portbury1, Sarah M Ronnebaum, Makhosazane Zungu, Cam Patterson, Monte S Willis.
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."Entities:
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Year: 2011 PMID: 22085703 PMCID: PMC3294005 DOI: 10.1016/j.yjmcc.2011.10.023
Source DB: PubMed Journal: J Mol Cell Cardiol ISSN: 0022-2828 Impact factor: 5.000