ROLE OF MEMBRANES IN THE ACTIVATION OF A NEW MULTIFUNCTIONAL PROTEIN-KINASE SYSTEM

被引:86
作者
TAKAI, Y [1 ]
KISHIMOTO, A [1 ]
IWASA, Y [1 ]
KAWAHARA, Y [1 ]
MORI, T [1 ]
NISHIZUKA, Y [1 ]
TAMURA, A [1 ]
FUJII, T [1 ]
机构
[1] KYOTO COLL PHARM,DEPT BIOCHEM,KYOTO 607,JAPAN
关键词
D O I
10.1093/oxfordjournals.jbchem.a132557
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A new multifunctional protein kinase, which normally exists as an inactive form in the soluble fraction in mammalian tissues, attaches to membranes to exhibit full enzymatic activity. A low concentration of Ca2+is absolutely necessary for this activation. This process is reversible. cAMP shows no effect. The active factors in membranes are phosphatidylinositol, phosphatidylserine, phosphatidic acid, diphosphatidylglycerol, and phosphatidylethanolamine in that order. Phosphatidylcholine and sphingomyelin are far less effective. Cytoplasmic as well as other membrane fractions from various tissues are active in supporting the enzymatic activity. A possible role of this Ca2+and phospholipid-activated protein kinase system in transmembrane control is proposed. © 1979 by The Journal of Biochemistry.
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页码:575 / 578
页数:4
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