Lefebvre Christophe, Largeau Céline, Michelet Xavier, Fourrage Cécile, Maniere Xavier, Matic Ivan, Legouis Renaud, Culetto Emmanuel
Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Univ. Paris-Sud, Université Paris-Saclay, Gif-sur-Yvette cedex 91198, France.
Brigham and Women's Hospital, 1 Jimmy Fund Way, Boston, MA 02115, USA.
J Cell Sci. 2016 Apr 1;129(7):1490-9. doi: 10.1242/jcs.178467. Epub 2016 Feb 18.
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.
肌浆网是由小管和池组成的网络,与收缩装置紧密相连,并调节横纹肌细胞内的Ca(2+)动态变化。尽管肌肉细胞反复收缩,肌浆网仍能通过尚在研究中的机制维持其形状和组织结构。内体分选转运复合体(ESCRT)在多个细胞过程中对组织膜亚结构域和改变膜拓扑结构至关重要。在此,我们首次报道ESCRT-II蛋白在秀丽隐杆线虫中对维持肌浆网完整性发挥作用。ESCRT-II蛋白与肌浆网标记物兰尼碱受体UNC-68共定位。ESCRT-II和UNC-68在肌浆网上的定位相互依赖。此外,对ESCRT-II突变体的特征分析揭示了肌浆网网络的碎片化,这与Ca(2+)动态变化的改变有关。我们的数据提供了证据表明ESCRT-II蛋白参与了肌浆网的塑形。