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Neuronal nitric oxide synthase localizes through multiple structural motifs to the sarcolemma in mouse myotubes
Author(s) -
Abdelmoity Ahmed,
Padre Roanna C,
Burzynski Kimberley E,
Stull James T,
Lau Kim S
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)02038-x
Subject(s) - sarcolemma , pdz domain , myogenesis , dystrophin , c2c12 , chemistry , microbiology and biotechnology , nitric oxide synthase , biochemistry , skeletal muscle , myocyte , biophysics , biology , anatomy , enzyme , gene
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.