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.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117 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
PMID28509956
show 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 Ca(2+) and diacylglycerol. Cytosolic Ca(2+) 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 Ca(2+)
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.