Journal article
Identification and Characterization of the Dystrophin Anchoring Site on β-Dystroglycan ()
The Journal of biological chemistry, Vol.270(45), pp.27305-27310
11/10/1995
DOI: 10.1074/jbc.270.45.27305
PMID: 7592992
Abstract
Dystrophin, the product of the Duchenne muscular dystrophy gene, is tightly associated with the sarcolemmal membrane to a large glycoprotein complex. One function of the dystrophin-glycoprotein complex is to link the cytoskeleton to the extracellular matrix in skeletal muscle. However, the molecular interactions of dystrophin with the membrane components of the dystrophin-glycoprotein complex are still elusive. Here, we demonstrate and characterize a specific interaction between β-dystroglycan and dystrophin. We show that skeletal muscle and brain dystrophin as well as brain dystrophin isoforms specifically bind to β-dystroglycan. To localize and characterize the dystrophin and β-dystroglycan interaction domains, we reconstituted the interaction in vitro using dystrophin fusion proteins and in vitro translated β-dystroglycan. We demonstrated that the 15 C-terminal amino acids of β-dystroglycan constituted a unique binding site for the second half of the hinge 4 and the cysteine-rich domain of dystrophin (amino acids 3054-3271). This dystrophin binding site is located in a proline-rich environment of β-dystroglycan within amino acids 880-895. The identification of the interaction sites in dystrophin and β-dystroglycan provides further insight into the structure and the molecular organization of the dystrophin-glycoprotein complex at the sarcolemma membrane and will be helpful for studying the pathogenesis of Duchenne muscular dystrophy.
Details
- Title: Subtitle
- Identification and Characterization of the Dystrophin Anchoring Site on β-Dystroglycan ()
- Creators
- Daniel Jung - Howard Hughes Medical Institute, University of Iowa College of Medicine, Iowa City, Iowa 52242Bin Yang - Howard Hughes Medical Institute, University of Iowa College of Medicine, Iowa City, Iowa 52242Jon Meyer - Howard Hughes Medical Institute, University of Iowa College of Medicine, Iowa City, Iowa 52242Jeffrey 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(45), pp.27305-27310
- DOI
- 10.1074/jbc.270.45.27305
- PMID
- 7592992
- NLM abbreviation
- J Biol Chem
- ISSN
- 0021-9258
- eISSN
- 1083-351X
- Publisher
- Elsevier Inc
- Language
- English
- Date published
- 11/10/1995
- Academic Unit
- Neurology; Molecular Physiology and Biophysics; Iowa Neuroscience Institute
- Record Identifier
- 9984068272302771
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