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Anchoring proteins for protein kinase C: a means for isozyme selectivity
Author(s) -
MochlyRosen Daria,
Gordon Adrienne S.
Publication year - 1998
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fsb2fasebj.12.1.35
Subject(s) - isozyme , protein kinase c , biology , biochemistry , subcellular localization , enzyme , function (biology) , gene , microbiology and biotechnology
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.—Mochly‐Rosen, D., Gordon, A. S. Anchoring proteins for protein kinase C: a means for isozyme selectivity. FASEB J. 12, 35–42 (1998)