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.

引用

页码：321 / 323

页数：3

共 18 条

[1]

AZHAEVA EV, 1987, BIOL MEMBRANY, V4, P980

[2]

BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3

[3] PROTEIN-PHOSPHORYLATION AND NEURONAL FUNCTION [J].