INOSITOL TRISPHOSPHATE RECEPTOR - PHOSPHORYLATION BY PROTEIN-KINASE-C AND CALCIUM CALMODULIN-DEPENDENT PROTEIN-KINASES IN RECONSTITUTED LIPID VESICLES

被引：224

作者：

FERRIS, CD

HUGANIR, RL

BREDT, DS

CAMERON, AM

SNYDER, SH

机构：

[1] JOHNS HOPKINS UNIV, SCH MED, DEPT NEUROSCI, BALTIMORE, MD 21205 USA

[2] JOHNS HOPKINS UNIV, SCH MED, DEPT PHARMACOL & MOLEC SCI, BALTIMORE, MD 21205 USA

[3] JOHNS HOPKINS UNIV, SCH MED, HOWARD HUGHES MED INST, BALTIMORE, MD 21205 USA

[4] JOHNS HOPKINS UNIV, SCH MED, DEPT PSYCHIAT & BEHAV SCI, BALTIMORE, MD 21205 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1991年 / 88卷 / 06期

关键词：

CAMP; INOSITOL PHOSPHOLIPID TURNOVER; DIACYLGLYCEROL; SERINE; THREONINE;

D O I：

10.1073/pnas.88.6.2232

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

We have previously demonstrated that the inositol 1,4,5-trisphosphate (IP3) receptor is phosphorylated by cyclic AMP-dependent protein kinase (PKA). In the present study, phosphorylation of IP3 receptors has been examined with purified receptor protein reconstituted in liposomes to remove detergent that can inhibit protein kinases. The IP3 receptor is stoichiometrically phosphorylated by protein kinase C (PKC) and Ca2+ calmodulin-dependent protein kinase II (CaM kinase II) as well as by PKA. Phosphorylation by the three enzymes is additive and involves different peptide sequences. Phosphorylation by PKC, which is stimulated by Ca2+ and diacylglycerol, and by CaM kinase II, which requires Ca2+, provides means whereby Ca2+ and diacylglycerol, formed during inositol phospholipid turnover, may regulate IP3 receptor physiology.

引用

页码：2232 / 2235

页数：4

共 22 条

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