Anchoring proteins for protein kinase C: a means for isozyme selectivity.
Anchoring proteins for protein kinase C: a means for isozyme selectivity.
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DOI：
10.1096/fasebj.12.1.35
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发表时间：
1998
期刊：
影响因子：
--
通讯作者：
D. Mochly‐Rosen;A. Gordon
中科院分区：
文献类型：
--
作者：
D. Mochly‐Rosen;A. Gordon
蛋白激酶C （PKC）同工酶包括一个相关的酶家族。这些同工酶在底物特异性或对活化剂的敏感性方面只有有限的差异。然而，在细胞内有多种同工酶介导同工酶特异性功能。差异亚细胞定位已被提出来解释这种特异性。当PKC家族成员被脂质衍生的第二信使激活时，它们从一个细胞区室转移到另一个细胞区室。同工酶特异性似乎部分是由每个PKC同工酶与特定锚定蛋白的关联介导的。这篇综述将涵盖与PKC同工酶锚定在特定亚细胞位点有关的蛋白质，PKC同工酶中介导与同工酶特异性锚定蛋白的蛋白-蛋白相互作用的结构域，以及干扰或促进这些蛋白-蛋白相互作用的肽的鉴定，从而改变单个同工酶的定位和功能。
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.