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A more recent version of this article appeared on July 1, 2004
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Submitted on March 23, 2004
Revised on April 23, 2004
Accepted on April 26, 2004
1 The G.W. Hooper Foundation, Department of Microbiology and Immunology and Departments of Biopharmaceutical Sciences and Pharmaceutical Chemistry, University of California, San Francisco, California, 94143-0552, U.S.A.
2 The Russell Grimwade School of Biochemistry and Molecular Biology, University of Melbourne, Vic. 3010, Melbourne, Australia
3 Department of Neurology, Institute of Clinical Medicine, University of Tsukuba, Tsukuba City, Japan
4 Kuusitie 67, Fin-40800 Vaajakoski, Finland
5 Department of Anatomy and Cardiovascular Research Institute, University of California San Francisco, San Francisco, California, 94143- 0452, U.S.A.
6 Institute for Molecular Biosciences, Center for Microscopy and Microanalysis, and School of Biomedical Sciences, University of Queensland, Brisbane 4072, Australia
* Corresponding author. E-mail address: fmarbro{at}itsa.ucsf.edu.
The muscle isoform of clathrin heavy chain, CHC22, has 85% sequence identity to the ubiquitously expressed CHC17, yet its expression pattern and function appear to be distinct from those of well-characterized clathrin-coated vesicles. In mature muscle CHC22 is preferentially concentrated at neuromuscular and myotendinous junctions, suggesting a role at sarcolemmal contacts with extracellular matrix. During myoblast differentiation, CHC22 expression is increased, initially localized with desmin and nestin, then preferentially segregated to the poles of fused myoblasts. CHC22 expression is also increased in regenerating muscle fibers with the same time course as embryonic myosin, indicating a role in muscle repair. CHC22 binds to sorting nexin 5 through a coiled-coil domain present in both partners, which is absent in CHC17 and coincides with the region on CHC17 that binds the regulatory light chain subunit. These differential binding data suggest a mechanism for the distinct functions of CHC22 relative to CHC17 in membrane traffic during muscle development, repair and at neuromuscular and myotendinous junctions.
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