Journal article
Sarcospan, the 25-kDa Transmembrane Component of the Dystrophin-Glycoprotein Complex
The Journal of biological chemistry, Vol.272(50), pp.31221-31224
12/12/1997
DOI: 10.1074/jbc.272.50.31221
PMID: 9395445
Abstract
The dystrophin-glycoprotein complex is a multisubunit protein complex that spans the sarcolemma and forms a link between the subsarcolemmal cytoskeleton and the extracellular matrix. Primary mutations in the genes encoding the proteins of this complex are associated with several forms of muscular dystrophy. Here we report the cloning and characterization of sarcospan, a unique 25-kDa member of this complex. Topology algorithms predict that sarcospan contains four transmembrane spanning helices with both N- and C-terminal domains located intracellularly. Phylogenetic analysis reveals that sarcospan's arrangement in the membrane as well as its primary sequence are similar to that of the tetraspan superfamily of proteins. Sarcospan co-localizes and co-purifies with the dystrophin-glycoprotein complex, demonstrating that it is an integral component of the complex. We also show that sarcospan expression is dramatically reduced in muscle from patients with Duchenne muscular dystrophy. This suggests that localization of sarcospan to the membrane is dependent on proper dystrophin expression. The gene encoding sarcospan maps to human chromosome 12p11.2, which falls within the genetic locus for congenital fibrosis of the extraocular muscle, an autosomal dominant muscular dystrophy.
Details
- Title: Subtitle
- Sarcospan, the 25-kDa Transmembrane Component of the Dystrophin-Glycoprotein Complex
- Creators
- Rachelle H Crosbie - Howard Hughes Medical Institute, Department of Physiology and Biophysics and the Department of Neurology, University of Iowa College of Medicine, Iowa City, Iowa 52242Jim Heighway - Paterson Institute for Cancer Research, Christie Hospital (NHS) Trust, Wilmslow Road, Manchester, M20 9BX, United KingdomDavid P Venzke - Howard Hughes Medical Institute, Department of Physiology and Biophysics and the Department of Neurology, University of Iowa College of Medicine, Iowa City, Iowa 52242Jane C Lee - Howard Hughes Medical Institute, Department of Physiology and Biophysics and the Department of Neurology, University of Iowa College of Medicine, Iowa City, Iowa 52242Kevin P Campbell - Howard Hughes Medical Institute, Department of Physiology and Biophysics and the Department of Neurology, University of Iowa College of Medicine, Iowa City, Iowa 52242
- Resource Type
- Journal article
- Publication Details
- The Journal of biological chemistry, Vol.272(50), pp.31221-31224
- DOI
- 10.1074/jbc.272.50.31221
- PMID
- 9395445
- NLM abbreviation
- J Biol Chem
- ISSN
- 0021-9258
- eISSN
- 1083-351X
- Publisher
- Elsevier Inc
- Language
- English
- Date published
- 12/12/1997
- Academic Unit
- Neurology; Molecular Physiology and Biophysics; Iowa Neuroscience Institute; Obstetrics and Gynecology
- Record Identifier
- 9984068388202771
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