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10.1007/s12551-013-0125-z

http://scihub22266oqcxt.onion/10.1007/s12551-013-0125-z
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C5427809!5427809!28509956
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suck abstract from ncbi


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pmid28509956      Biophys+Rev 2014 ; 6 (1): 3-14
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  • Classical protein kinases C are regulated by concerted interaction with lipids: the importance of phosphatidylinositol-4,5-bisphosphate #MMPMID28509956
  • Corbalán-García S; Gómez-Fernández JC
  • Biophys Rev 2014[Mar]; 6 (1): 3-14 PMID28509956show ga
  • 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.
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