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

被引：8

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

共 58 条

[1] Ausili A., Corbalan-Garcia S., Gomez-Fernandez J.C., Marsh D., Membrane docking of the C2 domain from protein kinase Calpha as seen by polarized ATR-IR. The role of PIP, Biochim Biophys Acta, 1808, 3, pp. 684-695, (2011)
[2] Banaszynski L.A., Wandless T.J., Conditional control of protein function, Chem Biol, 13, 1, pp. 11-21, (2006)
[3] Bell R.M., Hannun Y.A., Loomis C.R., Mechanism of regulation of protein kinase C by lipid second messengers, Symp Fundam Cancer Res, 39, pp. 145-156, (1986)
[4] Bolsover S.R., Gomez-Fernandez J.C., Corbalan-Garcia S., Role of the Ca2+/phosphatidylserine binding region of the C2 domain in the translocation of protein kinase Calpha to the plasma membrane, J Biol Chem, 278, 12, pp. 10282-10290, (2003)
[5] Castagna M., Takai Y., Kaibuchi K., Sano K., Kikkawa U., Nishizuka Y., Direct activation of calcium-activated, phospholipid-dependent protein kinase by tumor-promoting phorbol esters, J Biol Chem, 257, 13, pp. 7847-7851, (1982)
[6] Conesa-Zamora P., Gomez-Fernandez J.C., Corbalan-Garcia S., The C2 domain of protein kinase calpha is directly involved in the diacylglycerol-dependent binding of the C1 domain to the membrane, Biochim Biophys Acta, 1487, 2-3, pp. 246-254, (2000)
[7] Conesa-Zamora P., Lopez-Andreo M.J., Gomez-Fernandez J.C., Corbalan-Garcia S., Identification of the phosphatidylserine binding site in the C2 domain that is important for PKC alpha activation and in vivo cell localization, Biochemistry, 40, 46, pp. 13898-13905, (2001)
[8] Corbalan-Garcia S., Garcia-Garcia J., Rodriguez-Alfaro J.A., Gomez-Fernandez J.C., A new phosphatidylinositol 4,5-bisphosphate-binding site located in the C2 domain of protein kinase Calpha, J Biol Chem, 278, 7, pp. 4972-4980, (2003)
[9] Corbalan-Garcia S., Gomez-Fernandez J.C., Protein kinase C regulatory domains: the art of decoding many different signals in membranes, Biochim Biophys Acta, 1761, 7, pp. 633-654, (2006)
[10] Corbin J.A., Evans J.H., Landgraf K.E., Falke J.J., Mechanism of specific membrane targeting by C2 domains: localized pools of target lipids enhance Ca2+ affinity, Biochemistry, 46, 14, pp. 4322-4336, (2007)

← 1 2 3 4 5 6 →