Anchoring proteins for protein kinase C: a means for isozyme selectivity

被引:1
|
作者
Mochly-Rosen, D [1 ]
Gordon, AS
机构
[1] Stanford Univ, Sch Med, Dept Mol Pharmacol, Stanford, CA 94305 USA
[2] Univ Calif San Francisco, Ctr Neurobiol Addict, San Francisco, CA 94110 USA
[3] Univ Calif San Francisco, Ernest Gallo Clin & Res Ctr, Dept Neurol, San Francisco, CA 94110 USA
[4] Univ Calif San Francisco, Ernest Gallo Clin & Res Ctr, Dept Cellular & Mol Pharmacol, San Francisco, CA 94110 USA
来源
FASEB JOURNAL | 1998年 / 12卷 / 01期
关键词
PKC; RACK; RICK; localization;
D O I
暂无
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 protein-protein interaction with isozyme-specific anchoring proteins, and identification of peptides that interfere with or promote these protein-protein interactions, thus altering the localization and function of individual isozymes.
引用
收藏
页码:35 / 42
页数:8
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