Classical protein kinases C are regulated by concerted interaction with lipids: The importance of phosphatidylinositol-4,5-bisphosphate

被引：9

作者：

Corbalán-García S. ^{[1
]}

Gómez-Fernández J.C. ^{[1
]}

机构：

[1] Departamento de Bioquímica y Biología Molecular-A, Regional Campus of International Excellence Campus Mare Nostrum, Universidad de Murcia, 30080 Murcia

来源：

Biophysical Reviews | 2014年 / 6卷 / 1期

关键词：

C1; domain; C2; Diacylglycerol; Phosphatidylinositol-4,5-bisphosphate; Protein kinase C;

D O I：

10.1007/s12551-013-0125-z

中图分类号：

学科分类号：

摘要：

Classical protein kinase C (PKC) enzymes are known to be important factors in cell physiology both in terms of health and disease. They are activated by triggering signals that induce their translocation to membranes. The consensus view is that several secondary messengers are involved in this activation, such as cytosolic Ca2+ and diacylglycerol. Cytosolic Ca2+bridges the C2 domain to anionic phospholipids as phosphatidylserine in the membrane, and diacylglycerol binds to the C1 domain. Both diacylglycerol and the increase in Ca2+ concentration are assumed to arise from the extracellular signal that triggers the hydrolysis of phosphatidylinositol-4,5-bisphosphate. However, results obtained during the last decade indicate that this phosphoinositide itself is also responsible for modulating classical PKC activity and its localization in the plasma membrane. © 2013 International Union for Pure and Applied Biophysics (IUPAB) and Springer-Verlag Berlin Heidelberg.

引用

页码：3 / 14

页数：11

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