Phosphorylation of the triadin cytoplasmic domain by CaM protein kinase in rabbit fast-twitch muscle sarcoplasmic reticulum

被引：9

作者：

Colpo, P ^{[1
]}

Nori, A ^{[1
]}

Sacchetto, R ^{[1
]}

Damiani, E ^{[1
]}

Margreth, A ^{[1
]}

机构：

[1] Univ Padua, Dept Expt Biomed Sci, NRC Unit Muscle Biol & Physiopathol, I-35121 Padua, Italy

来源：

MOLECULAR AND CELLULAR BIOCHEMISTRY | 2001年 / 223卷 / 1-2期

关键词：

Ca2+-release channel; calmodulin protein kinase; sarcoplasmic reticulum; triadin;

D O I：

10.1023/A:1017987015807

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Skeletal muscle triadin is a sarcoplasmic reticulum (SR) membrane protein that had been shown to interact structurally and functionally at the cytoplasmic domain (amino acid residues 1-47) with the ryanodine receptor (RyR1), and to undergo phosphorylation by endogenous calmodulin protein kinase (CaM K II) in isolated terminal cisternae from rabbit fast-twitch muscle. Here we show that triadin cytoplasmic domain expressed as glutathione-S-transferase fusion protein, is a substrate of the protein kinase. This finding is corroborated by identification of a specific consensus sequence in the deduced amino sequence between residue 34 and 37 of triadin. Confirming the regulatory features of CaM K II, we show the phosphorylation of triadin cytoplasmic segment by the kinase, when converted to the autonomous form. We propose that triadin modulates RyR1 in a phosphorylation-dependent manner.

引用

页码：139 / 145

页数：7