Ontology highlight
ABSTRACT:
SUBMITTER: Vassilopoulos S
PROVIDER: S-EPMC4018784 | biostudies-other | 2014 May
REPOSITORIES: biostudies-other
Vassilopoulos Stéphane S Gentil Christel C Lainé Jeanne J Buclez Pierre-Olivier PO Franck Agathe A Ferry Arnaud A Précigout Guillaume G Roth Robyn R Heuser John E JE Brodsky Frances M FM Garcia Luis L Bonne Gisèle G Voit Thomas T Piétri-Rouxel France F Bitoun Marc M
The Journal of cell biology 20140505 3
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 diffe ...[more]