Neuronal nitric oxide synthase localizes through multiple structural motifs to the sarcolemma in mouse myotubes

被引:24
作者
Abdelmoity, A [1 ]
Padre, RC [1 ]
Burzynski, KE [1 ]
Stull, JT [1 ]
Lau, KS [1 ]
机构
[1] Univ Texas, SW Med Ctr, Dept Physiol, Dallas, TX 75390 USA
关键词
nitric oxide synthase; sarcolemmal binding; skeletal muscle; alpha-syntrophin; PDZ domain;
D O I
10.1016/S0014-5793(00)02038-X
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
In skeletal muscle, neuronal nitric oxide synthase is localized at the sarcolemma in association with the dystrophin glycoprotein complex: (DGC), The nNOS N-terminal 231 amino acids comprise a PDZ domain (residues 1-100) and a beta-hairpin finger loop (residues 101-130) which binds alpha-syntrophin located in the DGC, Endogenous nNOS and GFP-tagged nNOS localize to the sarcolemma in mouse C2C12 myotubes. Expression of GFP-tagged nNOS domains in C2C12 myotubes, reveals that the PDZ domain and the beta-hairpin finger loop of nNOS are independently capable of localizing to the sarcolemma of C2C12 myotubes. Binding studies indicate that alpha-syntrophin binds only to the beta-hairpin finger loop and not the PDZ domain of nNOS, nNOS may bind to proteins in addition to alpha-syntrophin at muscle sarcolemma, (C) 2000 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码:65 / 70
页数:6
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