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α1‐Syntrophin has distinct binding sites for actin and calmodulin
Author(s) -
Iwata Yuko,
Pan Yan,
Yoshida Tomokazu,
Hanada Hironori,
Shigekawa Munekazu
Publication year - 1998
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(98)00085-4
Subject(s) - calmodulin , chemistry , actin , microbiology and biotechnology , binding site , recombinant dna , biochemistry , biology , enzyme , gene
Overlay and co‐sedimentation assays using recombinant α1‐syntrophin proteins revealed that two regions of α1‐syntrophin, i.e. aa 274–315 and 449–505, contain high‐affinity binding sites for F‐actin ( K d 0.16–0.45 μM), although only a single high‐affinity site ( K d 0.35 μM) 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 α1‐syntrophin binds calmodulin at two distinct sites with high ( K d 15 nM) and low ( K d 0.3 μM) affinity.