Structural basis for plant plasma membrane protein dynamics and organization into functional nanodomains.
Structural basis for plant plasma membrane protein dynamics and organization into functional nanodomains.
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DOI：
10.7554/elife.26404
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发表时间：
2017-07-31
期刊：
影响因子：
7.7
通讯作者：
Mongrand S
中科院分区：
文献类型：
--
作者：
Gronnier J;Crowet JM;Habenstein B;Nasir MN;Bayle V;Hosy E;Platre MP;Gouguet P;Raffaele S;Martinez D;Grelard A;Loquet A;Simon-Plas F;Gerbeau-Pissot P;Der C;Bayer EM;Jaillais Y;Deleu M;Germain V;Lins L;Mongrand S
质膜是适应不断变化的条件的主要结构。域中的PM子区室化被认为是编排信号。然而，支配膜组织的机制大多没有特征。植物特异性REMORINs是调节激素串扰和宿主入侵的蛋白质。REM是通过称为REMORIN C-末端锚的未表征部分表征的最佳纳米结构域标记物。通过耦合生物物理方法，超分辨率显微镜和生理学，我们破译了一个原始的机制，调节动态和组织的纳米域。我们发现REMORIN的靶向作用不依赖于COP-II依赖性分泌途径，并由PI 4P和甾醇介导。REM-CA是赋予纳米结构域组织的非常规脂质结合基序。通过单粒子追踪对REM-CA突变体的分析表明，移动性和超分子组织对于免疫是至关重要的。这项研究提供了一个独特的机制洞察空间隔离的严格控制是至关重要的PM域的定义，必须支持生物功能。
Plasma Membrane is the primary structure for adjusting to ever changing conditions. PM sub-compartmentalization in domains is thought to orchestrate signaling. Yet, mechanisms governing membrane organization are mostly uncharacterized. The plant-specific REMORINs are proteins regulating hormonal crosstalk and host invasion. REMs are the best-characterized nanodomain markers via an uncharacterized moiety called REMORIN C-terminal Anchor. By coupling biophysical methods, super-resolution microscopy and physiology, we decipher an original mechanism regulating the dynamic and organization of nanodomains. We showed that targeting of REMORINis independent of the COP-II-dependent secretory pathway and mediated by PI4P and sterol. REM-CA is an unconventional lipid-binding motif that confers nanodomain organization. Analyzes of REM-CA mutants by single particle tracking demonstrate that mobility and supramolecular organization are critical for immunity. This study provides a unique mechanistic insight into how the tight control of spatial segregation is critical in the definition of PM domain necessary to support biological function.