Current Drug Targets

Francis J. Castellino
Kleiderer-Pezold Professor of Biochemistry
Director, W.M. Keck Center for Transgene Research
Dean Emeritus, College of Science
230 Raclin-Carmichael Hall, University of Notre Dame
Notre Dame, IN 46556


The Life and Death of Protein Kinase C

Author(s): Christine M. Gould, Alexandra C. Newton.


Protein kinase C (PKC) is a family of kinases that plays diverse roles in many cellular functions, notably proliferation, differentiation, and cell survival. PKC is processed by phosphorylation and regulated by cofactor binding and subcellular localization. Extensive detail is available on the molecular mechanisms that regulate the maturation, activation, and signaling of PKC. However, less information is available on how signaling is terminated both from a global perspective and isozyme-specific differences. To target PKC therapeutically, various ATP-competitive inhibitors have been developed, but this method has problems with specificity. One possible new approach to developing novel, specific therapeutics for PKC would be to target the signaling termination pathways of the enzyme. This review focuses on the new developments in understanding how PKC signaling is terminated and how current drug therapies as well as information obtained from the recent elucidation of various PKC structures and down-regulation pathways could be used to develop novel and specific therapeutics for PKC.

Keywords: family kinases, Protein Kinase C, cellular functions, proliferation, phosphorylation, molecular mechanisms, signaling termination pathways, current drug therapies

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Article Details

Year: 2008
Page: [614 - 625]
Pages: 12
DOI: 10.2174/138945008785132411
Price: $58