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a Department of Molecular Pharmacology, Stanford University, School of Medicine, Stanford, California 943055332, USA
b Departments of Neurology and Cellular and Molecular Pharmacology, Ernest Gallo Clinic and Research Center, Program in Neuroscience, and Center for the Neurobiology of Addiction, University of California, San Francisco, California 94110, USA
Protein kinase C (PKC) isozymes comprise a family of related enzymes. There are only limited differences between these isozymes in substrate specificity or sensitivity to activators. However, there are multiple isozymes within a cell mediating isozyme-specific functions. Differential subcellular localization has been proposed to explain this specificity. When members of the PKC family are activated by lipid-derived second messengers, they translocate from one cell compartment to another. Isozyme specificity appears to be mediated in part by association of each PKC isozyme with specific anchoring proteins. This review will cover the proteins involved in the anchoring of PKC isozymes at specific subcellular sites, the domains in the PKC isozymes that mediate proteinprotein interaction with isozyme-specific anchoring proteins, and identification of peptides that interfere with or promote these proteinprotein interactions, thus altering the localization and function of individual isozymes.Mochly-Rosen, D., Gordon, A. S. Anchoring proteins for protein kinase C: a means for isozyme selectivity. FASEB J. 12, 3542 (1998)
Key Words: PKC RACK RICK localization
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