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

Ahmed Abdelmoity, Roanna C. Padre, Kimberley E. Burzynski, James T. Stull, Kim S. Lau

Research output: Contribution to journalArticle

21 Scopus citations

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 languageEnglish (US)
Pages (from-to)65-70
Number of pages6
JournalFEBS Letters
Volume482
Issue number1-2
DOIs
StatePublished - 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

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