PHOSPHORYLATION OF THE SKELETAL-MUSCLE AMP-DEAMINASE BY PROTEIN KINASE-C

被引：23
|
作者：
TOVMASIAN, EK [1 ]
HAIRAPETIAN, RL [1 ]
BYKOVA, EV [1 ]
SEVERIN, SE [1 ]
HAROUTUNIAN, AV [1 ]
机构：
[1] MV LOMONOSOV FINE CHEM TECHNOL INST,MOSCOW,USSR
来源：
FEBS LETTERS | 1990年 / 259卷 / 02期
关键词：
AMP-deaminase; Phosphorylation; Protein kinase C;
D O I：
10.1016/0014-5793(90)80037-J
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：
Protein kinase C catalyzes phosphorylation of the rat skeletal muscle AMP-deaminase in the presence of calcium ions and phosphatidylserine. At the same time, the catalytic subunit of cAMP-dependent protein kinase fails to phosphorylate AMP-deaminase. Ca2+ phosphatidylserine-dependent phosphorylation decreases three-fold (from 0.6 to 0.2 mM) the Km value and does not affect Vmax Protein kinase C-induced phosphorylation of AMP-deaminase, besides ADP-ribosylation, is suggested to be involved in regulating the AMP-deaminase activity in vivo. © 1990.
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页码：321 / 323
页数：3
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