Identification of α-Syntrophin Binding to Syntrophin Triplet, Dystrophin, and Utrophin (*)

Identification of α-Syntrophin Binding to Syntrophin Triplet, Dystrophin, and Utrophin (*)
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α-肌营养蛋白与肌营养蛋白三联体、肌营养不良蛋白和肌养蛋白结合的鉴定 (*)

DOI:
10.1074/jbc.270.10.4975
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发表时间:
1995
期刊:
The Journal of Biological Chemistry
影响因子:
--
通讯作者:
K. Campbell
K. Campbell
中科院分区:
--
文献类型:
--
作者:
Bin Yang;D. Jung;J. Rafael;J. Chamberlain;K. Campbell

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Syntrophin represents three cytoplasmic components of the dystrophin-glycoprotein complex that links the cytoskeleton to the extracellular matrix in skeletal muscle. α-Syntrophin has now been translated in vitro and shown to associate directly with all three components of the syntrophin triplet and with dystrophin. The in vitro translated 71-kDa non-muscle dystrophin isoform, containing the cysteine-rich/C-terminal domain, can also interact with the syntrophin triplet. The syntrophin binding motif in dystrophin was localized to exons 73 and 74 including amino acids 3447-3481 by comparing the interactions of α-syntrophin and seven overlapping human dystrophin fusion proteins. More than one syntrophin interaction site in this binding motif was suggested. α-Syntrophin also interacts directly with a C-terminal utrophin fusion protein. α-Syntrophin is localized to the muscle sarcolemma as well as to the neuromuscular junction in control mouse muscle. However, similar to utrophin, α-syntrophin is only present at the neuromuscular junction in mdx mouse muscle in which dystrophin is absent. Our data suggest that α-syntrophin binds all syntrophin isoforms, and syntrophin directly interacts with dystrophin through more than one binding site in dystrophin exons 73 and 74 including amino acids 3447-3481.
DOI: 10.1093/hmg/3.10.1725
发表时间: 1994-10-01
影响因子: 3.5
作者:
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