scholarly journals Clathrin’s muscle-building regimen

2014 ◽  
Vol 205 (3) ◽  
pp. 285-285
Author(s):  
Ben Short
Keyword(s):  
Skeletal Muscle ◽  
Heavy Chain ◽  
Clathrin Heavy Chain ◽  
Membrane Scaffold

The clathrin heavy chain forms a membrane scaffold that organizes skeletal muscle sarcomeres.

scholarly journals Actin scaffolding by clathrin heavy chain is required for skeletal muscle sarcomere organization

2014 ◽  
Vol 205 (3) ◽  
pp. 377-393 ◽  
Author(s):  
Stéphane Vassilopoulos ◽  
Christel Gentil ◽  
Jeanne Lainé ◽  
Pierre-Olivier Buclez ◽  
Agathe Franck ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Heavy Chain ◽  
Neuromuscular Disorders ◽  
Contractile Force ◽  
Contractile Apparatus ◽  
Intracellular Membrane ◽  
Clathrin Heavy Chain ◽  
Attachment Sites ◽  
Main Component

The ubiquitous clathrin heavy chain (CHC), the main component of clathrin-coated vesicles, is well characterized for its role in intracellular membrane traffic and endocytosis from the plasma membrane (PM). Here, we demonstrate that in skeletal muscle CHC regulates the formation and maintenance of PM–sarcomere attachment sites also known as costameres. We show that clathrin forms large coated lattices associated with actin filaments and the muscle-specific isoform of α-actinin at the PM of differentiated myotubes. Depletion of CHC in myotubes induced a loss of actin and α-actinin sarcomeric organization, whereas CHC depletion in vivo induced a loss of contractile force due to the detachment of sarcomeres from the PM. Our results suggest that CHC contributes to the formation and maintenance of the contractile apparatus through interactions with costameric proteins and highlight an unconventional role for CHC in skeletal muscle that may be relevant to pathophysiology of neuromuscular disorders.

scholarly journals Actin scaffolding by clathrin heavy chain is required for skeletal muscle sarcomere organization

2014 ◽  
Vol 143 (6) ◽  
pp. 1436OIA20
Author(s):  
Stéphane Vassilopoulos ◽  
C. Gentil ◽  
J. Lainé ◽  
P Buclez ◽  
A. Franck ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Heavy Chain ◽  
Clathrin Heavy Chain

Structure of clathrin cages and coats in ice

1986 ◽  
Vol 44 ◽  
pp. 94-97
Author(s):  
G.P.A. Vigers ◽  
R.A. Crowther ◽  
B.M.F. Pearse
Keyword(s):  
Electron Microscopy ◽  
Heavy Chain ◽  
Outer Part ◽  
Coated Vesicles ◽  
Eukaryotic Cells ◽  
Coat Proteins ◽  
Terminal Domain ◽  
Clathrin Heavy Chain ◽  
Membrane Components

Clathrin forms the polyhedral cage of coated vesicles, which mediate the transfer of selected membrane components within eukaryotic cells. Clathrin cages and coated vesicles have been extensively studied by electron microscopy of negatively stained preparations and shadowed specimens. From these studies the gross morphology of the outer part of the polyhedral coat has been established and some features of the packing of clathrin trimers into the coat have also been described. However these previous studies have not revealed any internal details about the position of the terminal domain of the clathrin heavy chain, the location of the 100kd-50kd accessory coat proteins or the interactions of the coat with the enclosed membrane.

scholarly journals Single-nucleus RNA-seq and FISH identify coordinated transcriptional activity in mammalian myofibers

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Matthieu Dos Santos ◽  
Stéphanie Backer ◽  
Benjamin Saintpierre ◽  
Brigitte Izac ◽  
Muriel Andrieu ◽  
...  
Keyword(s):  
Gene Expression ◽  
Skeletal Muscle ◽  
Transcription Factors ◽  
Neuromuscular Junction ◽  
Heavy Chain ◽  
Transcriptional Activity ◽  
Rna Seq ◽  
Hybrid Fibers ◽  
Adult Mice ◽  
Single Nucleus

Abstract Skeletal muscle fibers are large syncytia but it is currently unknown whether gene expression is coordinately regulated in their numerous nuclei. Here we show by snRNA-seq and snATAC-seq that slow, fast, myotendinous and neuromuscular junction myonuclei each have different transcriptional programs, associated with distinct chromatin states and combinations of transcription factors. In adult mice, identified myofiber types predominantly express either a slow or one of the three fast isoforms of Myosin heavy chain (MYH) proteins, while a small number of hybrid fibers can express more than one MYH. By snRNA-seq and FISH, we show that the majority of myonuclei within a myofiber are synchronized, coordinately expressing only one fast Myh isoform with a preferential panel of muscle-specific genes. Importantly, this coordination of expression occurs early during post-natal development and depends on innervation. These findings highlight a previously undefined mechanism of coordination of gene expression in a syncytium.

scholarly journals Characterization of a Temperature-Sensitive Vertebrate Clathrin Heavy Chain Mutant as a Tool to Study Clathrin-Dependent Events In Vivo

PLoS ONE ◽  
2010 ◽  
Vol 5 (8) ◽  
pp. e12017 ◽  
Author(s):  
Petra Neumann-Staubitz ◽  
Stephanie L. Hall ◽  
Joseph Kuo ◽  
Antony P. Jackson
Keyword(s):  
Heavy Chain ◽  
Temperature Sensitive ◽  
Clathrin Heavy Chain

Myosin Heavy Chain Expression in Skeletal Muscle Autografts under Neural or Aneural Conditions

1998 ◽  
Vol 75 (2) ◽  
pp. 135-147 ◽  
Author(s):  
Kotaro Yoshimura ◽  
William M. Kuzon ◽  
Kiyonori Harii
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain

The effect of glucocorticoids on the myosin heavy chain isoforms’ turnover in skeletal muscle

2003 ◽  
Vol 86 (2) ◽  
pp. 201-206 ◽  
Author(s):  
Teet Seene ◽  
Priit Kaasik ◽  
Ando Pehme ◽  
Karin Alev ◽  
Eva-Maria Riso
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Myosin Heavy Chain Isoforms
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