Glycoprotein‐binding site of dystrophin is confined to the cysteine‐rich domain and the first half of the carboxy‐terminal domain
- 17 August 1992
- journal article
- Published by Wiley in FEBS Letters
- Vol. 308 (2) , 154-160
- https://doi.org/10.1016/0014-5793(92)81265-n
Abstract
Dystrophin, a protein product of the Duchenne muscular dystrophy gene, is thought to associate with the muscle membrane by way of a glycoprotein complex which was co‐purified with dystrophin. Here, we firstly demonstrate direct biochemical evidence for association of the carboxy‐terminal region of dystrophin with the glycoprotein complex. The binding site is found to lie further inward than previously expected and confined to the cysteine‐rich domain and the first half of the carboxy‐terminal domain. Since this portion corresponds well to the region that, when missing results in severe phenotypes, our findings may provide it molecular basis of the disease.Keywords
This publication has 31 references indexed in Scilit:
- Are cysteine-rich and COOH-terminal domains of dystrophin critical for sarcolemmal localization?Journal of Clinical Investigation, 1992
- Primary structure of dystrophin-associated glycoproteins linking dystrophin to the extracellular matrixNature, 1992
- Is the carboxyl‐terminus of dystrophin required for membrane association? A novel, severe case of duchenne muscular dystrophyAnnals of Neurology, 1991
- Expression of dystrophin on the cell surface membrane of intrafusal fibers of human skeletal muscleProtoplasma, 1989
- Alternative splicing of human dystrophin mRNA generates isoforms at the carboxy terminusNature, 1989
- Dystrophin abnormalities in Duchenne/Becker muscular dystrophyNeuron, 1989
- Negative immunostaining of Duchenne muscular dystrophy(DMD) and mdx muscle surface membrane with antibody against synthetic peptide fragment predicted from DMD cDNA.Proceedings of the Japan Academy, Series B, 1988
- Complete cloning of the duchenne muscular dystrophy (DMD) cDNA and preliminary genomic organization of the DMD gene in normal and affected individualsCell, 1987
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS*Annals of the New York Academy of Sciences, 1964