The ESCRT-II proteins are involved in shaping the sarcoplasmic reticulum in C. elegans
Author(s) -
Christophe Lefebvre,
Céline Largeau,
Xavier Michelet,
Cécile Fourrage,
Xavier Manière,
Ivan Matić,
Renaud Legouis,
Emmanuel Culetto
Publication year - 2016
Publication title -
journal of cell science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.384
H-Index - 278
eISSN - 1477-9137
pISSN - 0021-9533
DOI - 10.1242/jcs.178467
Subject(s) - escrt , endoplasmic reticulum , biology , microbiology and biotechnology , ryanodine receptor , endosome , calcium binding protein , membrane protein , biochemistry , calcium , membrane , chemistry , intracellular , organic chemistry
The sarcoplasmic reticulum is a network of tubules and cisternae localized in close association with the contractile apparatus, and regulates Ca(2+)dynamics within striated muscle cell. The sarcoplasmic reticulum maintains its shape and organization despite repeated muscle cell contractions, through mechanisms which are still under investigation. The ESCRT complexes are essential to organize membrane subdomains and modify membrane topology in multiple cellular processes. Here, we report for the first time that ESCRT-II proteins play a role in the maintenance of sarcoplasmic reticulum integrity inC. elegans ESCRT-II proteins colocalize with the sarcoplasmic reticulum marker ryanodine receptor UNC-68. The localization at the sarcoplasmic reticulum of ESCRT-II and UNC-68 are mutually dependent. Furthermore, the characterization of ESCRT-II mutants revealed a fragmentation of the sarcoplasmic reticulum network, associated with an alteration of Ca(2+)dynamics. Our data provide evidence that ESCRT-II proteins are involved in sarcoplasmic reticulum shaping.
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