Journal article
Identification of α-Syntrophin Binding to Syntrophin Triplet, Dystrophin, and Utrophin (∗)
The Journal of biological chemistry, Vol.270(10), pp.4975-4978
03/10/1995
DOI: 10.1074/jbc.270.10.4975
PMID: 7890602
Abstract
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.
Details
- Title: Subtitle
- Identification of α-Syntrophin Binding to Syntrophin Triplet, Dystrophin, and Utrophin (∗)
- Creators
- Bin Yang - Howard Hughes Medical Institute, University of Iowa College of Medicine, Iowa City, Iowa 52242Daniel Jung - Howard Hughes Medical Institute, University of Iowa College of Medicine, Iowa City, Iowa 52242Jill A Rafael - Department of Human Genetics, University of Michigan Medical School, Ann Arbor, Michigan 48109Jeffrey S Chamberlain - Department of Human Genetics, University of Michigan Medical School, Ann Arbor, Michigan 48109Kevin P Campbell - Howard Hughes Medical Institute, University of Iowa College of Medicine, Iowa City, Iowa 52242
- Resource Type
- Journal article
- Publication Details
- The Journal of biological chemistry, Vol.270(10), pp.4975-4978
- DOI
- 10.1074/jbc.270.10.4975
- PMID
- 7890602
- NLM abbreviation
- J Biol Chem
- ISSN
- 0021-9258
- eISSN
- 1083-351X
- Publisher
- Elsevier Inc
- Language
- English
- Date published
- 03/10/1995
- Academic Unit
- Neurology; Molecular Physiology and Biophysics; Iowa Neuroscience Institute
- Record Identifier
- 9984068385002771
Metrics
14 Record Views