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EMBO Rep. 2011 Jul 8;12(8):785-96. doi: 10.1038/embor.2011.139.

Protein kinase D: coupling extracellular stimuli to the regulation of cell physiology.

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1
Department of Molecular Pharmacology, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, New York 10461, USA.

Abstract

Protein kinase D (PKD) mediates the actions of stimuli that promote diacylglycerol (DAG) biogenesis. By phosphorylating effectors that regulate transcription, fission and polarized transport of Golgi vesicles, as well as cell migration and survival after oxidative stress, PKDs substantially expand the range of physiological processes controlled by DAG. Dysregulated PKDs have been linked to pathologies including heart hypertrophy and cancer invasiveness. Our understanding of PKD regulation by trans- and autophosphorylation, as well as the subcellular dynamics of PKD substrate phosphorylation, have increased markedly. Selective PKD inhibitors provide new, powerful tools for elucidating the physiological roles of PKDs and potentially treating cardiac disease and cancer.

PMID:
21738220
PMCID:
PMC3147268
DOI:
10.1038/embor.2011.139
[Indexed for MEDLINE]
Free PMC Article
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