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FEBS Lett. 1998 Feb 20;423(2):173-7.

Alpha1-syntrophin has distinct binding sites for actin and calmodulin.

Author information

1
Department of Molecular Physiology, National Cardiovascular Center Research Institute, Suita, Osaka, Japan.

Abstract

Overlay and co-sedimentation assays using recombinant alpha1-syntrophin proteins revealed that two regions of alpha1-syntrophin, i.e. aa 274-315 and 449-505, contain high-affinity binding sites for F-actin (Kd 0.16-0.45 microM), although only a single high-affinity site (Kd 0.35 microM) was detected in the recombinant full-length syntrophin. We also found that actomyosin fractions prepared from both cardiac and skeletal muscle contain proteins recognized by anti-syntrophin antibody. These data suggest a novel role for syntrophin as an actin binding protein, which may be important for the function of the dystrophin-glycoprotein complex or for other cell functions. We also found that alpha1-syntrophin binds calmodulin at two distinct sites with high (Kd 15 nM) and low (Kd 0.3 microM) affinity.

PMID:
9512352
DOI:
10.1016/s0014-5793(98)00085-4
[Indexed for MEDLINE]
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