Journal article
Caveolin-3 is not an integral component of the dystrophin glycoprotein complex
FEBS letters, Vol.427(2), pp.279-282
1998
DOI: 10.1016/S0014-5793(98)00442-6
PMID: 9607328
Abstract
The dystrophin-glycoprotein complex is a multi-subunit protein complex that spans the muscle plasma membrane (sarcolemma) and forms a link between the intracellular cytoskeleton and the extracellular matrix. Caveolin-3, the muscle specific form of caveolin, is also a major structural and regulatory integral membrane protein found at the sarcolemma. Oligomers of caveolin-3 form the structural framework for small membrane pockets known as caveolae. We directly examined whether caveolin-3 is an integral component of the dystrophin-glycoprotein complex by examining four common biochemical and cellular properties of proteins integrally bound to the dystrophin-glycoprotein complex. We found that caveolin-3 de-enriches with partial purification of the dystrophin-glycoprotein complex although a small amount of caveolin-3 is present. Sucrose gradient fractionation and laminin affinity chromatography completely separate this residual caveolin-3 from the core components of the dystrophin-glycoprotein complex. We also show that caveolin-3 expression at the sarcolemma is not reduced in patients with primary mutations in either dystrophin or the sarcoglycans. This data demonstrates that localization of caveolin-3 to the sarcolemma occurs independently of the dystrophin-glycoprotein complex and that caveolin-3 is not an integral component of the dystrophin-glycoprotein complex.
Details
- Title: Subtitle
- Caveolin-3 is not an integral component of the dystrophin glycoprotein complex
- Creators
- Rachelle H Crosbie - Howard Hughes Medical Institute, Department of Physiology and Biophysics, Department of Neurology, University of Iowa College of Medicine, 400 Eckstein Medical Research Building, Iowa City, IA 52242, USAHiroki Yamada - Howard Hughes Medical Institute, Department of Physiology and Biophysics, Department of Neurology, University of Iowa College of Medicine, 400 Eckstein Medical Research Building, Iowa City, IA 52242, USADavid P Venzke - Howard Hughes Medical Institute, Department of Physiology and Biophysics, Department of Neurology, University of Iowa College of Medicine, 400 Eckstein Medical Research Building, Iowa City, IA 52242, USAMichael P Lisanti - Department of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, NY 10461, USAKevin P Campbell - Howard Hughes Medical Institute, Department of Physiology and Biophysics, Department of Neurology, University of Iowa College of Medicine, 400 Eckstein Medical Research Building, Iowa City, IA 52242, USA
- Resource Type
- Journal article
- Publication Details
- FEBS letters, Vol.427(2), pp.279-282
- Publisher
- Elsevier B.V
- DOI
- 10.1016/S0014-5793(98)00442-6
- PMID
- 9607328
- ISSN
- 0014-5793
- eISSN
- 1873-3468
- Language
- English
- Date published
- 1998
- Academic Unit
- Neurology; Molecular Physiology and Biophysics; Iowa Neuroscience Institute
- Record Identifier
- 9984068278002771
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