4.5 Review

The substrates and binding partners of protein kinase Cε

Journal

BIOCHEMICAL JOURNAL
Volume 427, Issue -, Pages 189-196

Publisher

PORTLAND PRESS LTD
DOI: 10.1042/BJ20091302

Keywords

anchoring protein; drug discovery; phosphorylation; protein kinase C epsilon (PKC epsilon); signalling

Funding

  1. National Institutes of Health [AA013588, NS053709, AA017072, DA027948]
  2. U.S. Department of the Army [PT075682]
  3. State of California for medical research on alcohol and substance abuse through the University of California at San Francisco

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The epsilon isoform of protein kinase C (PKC epsilon) has important roles in the function of the cardiac, immune and nervous systems. As a result of its diverse actions. PKC epsilon is the target of active drug-discovery programmes. A major research locus is to identify signalling cascades that include PKC epsilon and the substrates that PKC epsilon regulates. In the present review, we identify and discuss those proteins that have been conclusively shown to be direct substrates of PKC epsilon by the best currently available means. We will also describe binding partners that anchor PKC epsilon near its substrates. We review the consequences of substrate phosphorylation and discuss cellular mechanisms by which target specificity is achieved. We begin with a brief overview of the biology of PKC epsilon and methods for substrate identification, and proceed with a discussion of substrate categories to identify common themes that emerge and how these may be used to guide future studies.

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