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REM1.3 的磷酸化状态决定了其在限制 PVX 细胞间运动时的质膜纳米域组织和活性。

REM1.3's phospho-status defines its plasma membrane nanodomain organization and activity in restricting PVX cell-to-cell movement.

机构信息

Laboratoire de Biogenèse Membranaire (LBM), UMR 5200, CNRS/Université de Bordeaux, Bordeaux, France.

Institute of Plant Sciences Paris Saclay (IPS2), CNRS, INRA, Université Paris-Sud, Université d'Evry, Université Paris-Saclay, Université Paris-Diderot, Sorbonne Paris-Cité, Plateau du Moulon, France.

出版信息

PLoS Pathog. 2018 Nov 12;14(11):e1007378. doi: 10.1371/journal.ppat.1007378. eCollection 2018 Nov.

DOI:10.1371/journal.ppat.1007378
PMID:30419072
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6258466/
Abstract

Plants respond to pathogens through dynamic regulation of plasma membrane-bound signaling pathways. To date, how the plant plasma membrane is involved in responses to viruses is mostly unknown. Here, we show that plant cells sense the Potato virus X (PVX) COAT PROTEIN and TRIPLE GENE BLOCK 1 proteins and subsequently trigger the activation of a membrane-bound calcium-dependent kinase. We show that the Arabidopsis thaliana CALCIUM-DEPENDENT PROTEIN KINASE 3-interacts with group 1 REMORINs in vivo, phosphorylates the intrinsically disordered N-terminal domain of the Group 1 REMORIN REM1.3, and restricts PVX cell-to-cell movement. REM1.3's phospho-status defines its plasma membrane nanodomain organization and is crucial for REM1.3-dependent restriction of PVX cell-to-cell movement by regulation of callose deposition at plasmodesmata. This study unveils plasma membrane nanodomain-associated molecular events underlying the plant immune response to viruses.

摘要

植物通过对质膜结合信号通路的动态调节来响应病原体。迄今为止,植物质膜如何参与对病毒的响应在很大程度上尚不清楚。在这里,我们表明植物细胞感知马铃薯病毒 X (PVX) 外壳蛋白和三联基因块 1 蛋白,随后触发质膜结合钙依赖性激酶的激活。我们表明,拟南芥钙依赖性蛋白激酶 3 在体内与组 1 REMORINs 相互作用,磷酸化组 1 REMORIN REM1.3 的无规则卷曲的 N 端结构域,并限制 PVX 的细胞间运动。REM1.3 的磷酸化状态决定了其质膜纳米域的组织,并且对于通过调节质膜通道处的胼胝质沉积来调控 REM1.3 依赖的 PVX 细胞间运动的限制至关重要。这项研究揭示了植物对病毒免疫反应中与质膜纳米域相关的分子事件。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/825e/6258466/bef5d1075990/ppat.1007378.g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/825e/6258466/1d7277681e6b/ppat.1007378.g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/825e/6258466/757d8fedc00c/ppat.1007378.g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/825e/6258466/72d19aad6312/ppat.1007378.g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/825e/6258466/26fcb5de02c2/ppat.1007378.g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/825e/6258466/bae56b66285e/ppat.1007378.g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/825e/6258466/bef5d1075990/ppat.1007378.g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/825e/6258466/1d7277681e6b/ppat.1007378.g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/825e/6258466/757d8fedc00c/ppat.1007378.g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/825e/6258466/72d19aad6312/ppat.1007378.g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/825e/6258466/26fcb5de02c2/ppat.1007378.g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/825e/6258466/bae56b66285e/ppat.1007378.g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/825e/6258466/bef5d1075990/ppat.1007378.g006.jpg

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