Institute of Chemistry & Biology of Membranes & Nanoobjects (UMR5248 CBMN), IECB, CNRS, Universite Bordeaux, Institut Polytechnique Bordeaux, All. Geoffroy Saint-Hilaire, 33600 Pessac, France.
Laboratoire de Biogènese Membranaire - UMR 5200 - CNRS, Université de Bordeaux, 71 Avenue Edouard Bourlaux, 33883 Villenave d'Ornon Cédex, France.
J Struct Biol. 2019 Apr 1;206(1):12-19. doi: 10.1016/j.jsb.2018.02.003. Epub 2018 Feb 23.
REMORINs are nanodomain-organized proteins located in the plasma membrane and involved in cellular responses in plants. The dynamic assembly of the membrane nanodomains represents an essential tool of the versatile membrane barriers to control and modulate cellular functions. Nevertheless, the assembly mechanisms and protein organization strategies of nanodomains are poorly understood and many structural aspects are difficult to visualize. Using an ensemble of biophysical approaches, including solid-state nuclear magnetic resonance, cryo-electron microscopy and in vivo confocal imaging, we provide first insights on the role and the structural mechanisms of REMORIN trimerization. Our results suggest that the formation of REMORIN coiled-coil trimers is essential for membrane recruitment and promotes REMORIN assembly in vitro into long filaments by trimer-trimer interactions that might participate in nanoclustering into membrane domains in vivo.
REMO 蛋白是定位于质膜的纳米域组织蛋白，参与植物的细胞反应。膜纳米域的动态组装代表了多功能膜屏障控制和调节细胞功能的重要工具。然而，纳米域的组装机制和蛋白质组织策略还了解甚少，许多结构方面难以可视化。我们使用一系列生物物理方法，包括固态核磁共振、冷冻电子显微镜和体内共聚焦成像，首次提供了 REMORIN 三聚体作用和结构机制的见解。我们的结果表明，REMO 卷曲螺旋三聚体的形成对于膜募集是必不可少的，并通过三聚体-三聚体相互作用促进体外 REMORIN 组装成长丝，这种相互作用可能参与体内膜域的纳米聚类。
