Abstract
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 β-hairpin finger loop (residues 101-130) which binds α-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 β-hairpin finger loop of nNOS are independently capable of localizing to the sarcolemma of C2C12 myotubes. Binding studies indicate that α-syntrophin binds only to the β-hairpin finger loop and not the PDZ domain of nNOS. nNOS may bind to proteins in addition to α-syntrophin at muscle sarcolemma. Copyright (C) 2000 Federation of European Biochemical Societies.
Original language | English (US) |
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Pages (from-to) | 65-70 |
Number of pages | 6 |
Journal | FEBS Letters |
Volume | 482 |
Issue number | 1-2 |
DOIs | |
State | Published - Sep 29 2000 |
Keywords
- Nitric oxide synthase
- PDZ domain
- Sarcolemmal binding
- Skeletal muscle
- α-Syntrophin
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology