Clathrin isoform CHC22, a component of neuromuscular and myotendinous junctions, binds sorting nexin 5 and has increased expression during myogenesis and muscle regeneration

Towler, Mhairi C., Gleeson, Paul A., Hoshino, Sachiko, Rahkila, Paavo, Manalo, Venus, Ohkoshi, Norio, Ordahl, Charles, Parton, Robert G. and Brodsky, Frances M. (2004) Clathrin isoform CHC22, a component of neuromuscular and myotendinous junctions, binds sorting nexin 5 and has increased expression during myogenesis and muscle regeneration. Molecular Biology of The Cell, 15 7: 3181-3195. doi:10.1091/mbc.E04-03-0249

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Author Towler, Mhairi C.
Gleeson, Paul A.
Hoshino, Sachiko
Rahkila, Paavo
Manalo, Venus
Ohkoshi, Norio
Ordahl, Charles
Parton, Robert G.
Brodsky, Frances M.
Title Clathrin isoform CHC22, a component of neuromuscular and myotendinous junctions, binds sorting nexin 5 and has increased expression during myogenesis and muscle regeneration
Journal name Molecular Biology of The Cell   Check publisher's open access policy
ISSN 1059-1524
Publication date 2004
Sub-type Article (original research)
DOI 10.1091/mbc.E04-03-0249
Open Access Status File (Publisher version)
Volume 15
Issue 7
Start page 3181
End page 3195
Total pages 15
Place of publication Bethesda, USA
Publisher American Society for Biology
Collection year 2004
Language eng
Subject C1
270104 Membrane Biology
780106 Political science and public policy
Abstract 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 and 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.
Keyword Cell Biology
Heavy-chain Gene
Skeletal-muscle
Light-chains
Dystrophin
Disruption
Family
Differentiation
Dystroglycan
Organization
Endocytosis
Q-Index Code C1

 
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Created: Wed, 15 Aug 2007, 04:37:09 EST