ArticleJournal of cell science2016
The ESCRT-II proteins are involved in shaping the sarcoplasmic reticulum in C. elegans.
Article in Journal of cell science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed.
- Review
- Post-Transcriptional Modifications of RNA as Regulators of Apoptosis in Glioblastoma.International journal of molecular sciences · 2022Review
- YTHDC1-mediated VPS25 regulates cell cycle by targeting JAK-STAT signaling in human glioma cells.Cancer cell international · 2021Article
- Pluronic gel-based burrowing assay for rapid assessment of neuromuscular health in C. elegans.Scientific reports · 2019Article
- Three-Dimensional Surface Rendering of ESCRT Proteins Microscopy Data Using UCSF Chimera Software.Methods in molecular biology (Clifton, N.J.) · 2019Article
- Subcellular Localization of ESCRT-II in the Nematode C. elegans by Correlative Light Electron Microscopy.Methods in molecular biology (Clifton, N.J.) · 2019Article
- ESCRT-dependent cargo sorting at multivesicular endosomes.Seminars in cell & developmental biology · 2018Review
- Membrane Binding by CHMP7 Coordinates ESCRT-III-Dependent Nuclear Envelope Reformation.Current biology : CB · 2016Article
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Authors and funding
8 authors.
Funding
Abstract
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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