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Clathrin isoform CHC22, a component of neuromuscular and myotendinous junctions, binds sorting nexin 5 and has increased expression during myogenesis and muscle regeneration
- Source :
- Towler, MC; Gleeson, PA; Hoshino, S; Rahkila, P; Ohkoshi, N; Ordahl, CP; et al.(2017). 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. doi: 10.1091/mbc.E04-03-0249. UC San Francisco: Retrieved from: http://www.escholarship.org/uc/item/0k721808
- Publication Year :
- 2017
- Publisher :
- eScholarship, University of California, 2017.
-
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.
- Subjects :
- Animals Carrier Proteins/*metabolism Cell Line Clathrin/*metabolism Clathrin Heavy Chains/analysis/genetics/*metabolism Cobra Cardiotoxin Proteins/pharmacology Desmin/analysis/metabolism Humans Integrins/analysis/metabolism Intermediate Filament Proteins/analysis/metabolism *Muscle Development Muscle Proteins/analysis/genetics/*metabolism Muscle
Skeletal/growth & development/metabolism/*physiology Nerve Tissue Proteins/analysis/metabolism Nestin Neuromuscular Junction/chemistry/*metabolism Protein Transport *Regeneration Sorting Nexins Tendons/immunology/metabolism Two-Hybrid System Techniques Vesicular Transport Proteins
Animals Carrier Proteins/*metabolism Cell Line Clathrin/*metabolism Clathrin Heavy Chains/analysis/genetics/*metabolism Cobra Cardiotoxin Proteins/pharmacology Desmin/analysis/metabolism Humans Integrins/analysis/metabolism Intermediate Filament Proteins/analysis/metabolism *Muscle Development Muscle Proteins/analysis/genetics/*metabolism Muscle, Skeletal/growth & development/metabolism/*physiology Nerve Tissue Proteins/analysis/metabolism Nestin Neuromuscular Junction/chemistry/*metabolism Protein Transport *Regeneration Sorting Nexins Tendons/immunology/metabolism Two-Hybrid System Techniques Vesicular Transport Proteins
Biological Sciences
Medical and Health Sciences
Developmental Biology
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Journal :
- Towler, MC; Gleeson, PA; Hoshino, S; Rahkila, P; Ohkoshi, N; Ordahl, CP; et al.(2017). 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. doi: 10.1091/mbc.E04-03-0249. UC San Francisco: Retrieved from: http://www.escholarship.org/uc/item/0k721808
- Accession number :
- edsair.dedup.wf.001..675ee23bce0e89da23df6d18b79500bd