GLYCINERGIC LIGANDS MODULATE THE RATE OF PHOSPHORYLATION OF THE GLYCINE RECEPTOR BY PROTEIN-KINASE-C

被引：7

作者：

VAELLO, ML ^{[1
]}

RUIZGOMEZ, A ^{[1
]}

MAYOR, F ^{[1
]}

机构：

[1] Univ Autonoma Madrid, CSIC, Ctr Biol Mol Severo Ochoa, E-28049 Madrid, SPAIN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1992年 / 188卷 / 02期

关键词：

D O I：

10.1016/0006-291X(92)91129-E

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：

The α subunit of the glycine receptor purified from rat spinal cord is rapidly and specifically phosphorylated by protein kinase C (Ruiz-Gómez et al., (1991) J. Biol. Chem. 266, 559-566). We report here that the rate of phosphorylation of the glycine receptor by this kinase is higher in the presence of agonists (glycine, β-alanine) than in the presence of antagonists (strychnine, RU-5135). These results suggest that activated glycine receptors would be a preferential target for functional regulation through phosphorylation mechanisms. © 1992.

引用

页码：813 / 819

页数：7

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