Cytosolic WPRa4 and Plastoskeletal PMI4 Proteins Mediate Touch Response in a Model Organism Arabidopsis.

IF 6.1 2区生物学 Q1 BIOCHEMICAL RESEARCH METHODS

Molecular & Cellular Proteomics Pub Date : 2025-06-11 DOI:10.1016/j.mcpro.2025.101015

Kebin Wu, Nan Yang, Jia Ren, Shichang Liu, Kai Wang, Shuaijian Dai, Yinglin Lu, Yuxing An, Fuyun Tian, Zhaobing Gao, Zhu Yang, Yage Zhang, Weichuan Yu, Ning Li

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引用次数: 0

Abstract

To elucidate the early signaling components involved in thigmomorphogenesis in Arabidopsis thaliana, we combined microscopy and proximity-labeling (PL)-based quantitative biotinylproteomics to characterize the touch-responsive putative cytoskeleton-interacting protein WPRa4. Our findings revealed that WPRa4 localizes near plastids and interacts with cytosolic Plastid Movement-Impaired (PMI) proteins and a plastidic translocon component, suggesting a cytoskeleton-plastid network in mechanosensing. Bioinformatic analysis of PL and cross-linking mass spectrometry (XL-MS) data identified PMI4 as a key mediator, with pmi4 mutants lacking touch-induced bolting delay, rosette size reduction, and Ca²⁺ oscillations. Transcriptomics further showed that PMI4 regulates touch-responsive and jasmonic acid (JA)-associated genes, such as LOX2. We propose a molecular model where interconnected Cytoskeleton-Plastoskeleton Continuum (CPC) proteins act as early mechanosensors, integrating the touch responses of plant aerial organs with calcium signaling and transcriptional reprogramming in Arabidopsis.

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拟南芥模型生物细胞质WPRa4和塑性骨骼PMI4蛋白介导触摸反应。

为了阐明拟南芥thigmomorphogenesis中涉及的早期信号成分，我们结合显微镜和基于接近标记（PL）的定量生物素蛋白质组学来表征触摸响应的假定细胞骨架相互作用蛋白WPRa4。我们的研究结果表明，WPRa4定位于质体附近，并与细胞质质体运动受损蛋白（PMI）和质体转位成分相互作用，表明在机械传感中存在细胞骨架-质体网络。生物信息学分析和交联质谱（XL-MS）数据确定PMI4是关键的中介，PMI4突变体缺乏触摸诱导的栓接延迟、玫瑰花结大小减小和Ca2+振荡。转录组学进一步表明，PMI4调控触摸响应和茉莉酸（JA）相关基因，如LOX2。我们提出了一个分子模型，其中相互连接的细胞骨架-塑性骨架连续体（CPC）蛋白作为早期的机械传感器，将植物空中器官的触摸反应与钙信号和转录重编程结合起来。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Molecular & Cellular Proteomics 生物-生化研究方法

CiteScore

11.50

自引率

4.30%

发文量

131

审稿时长

84 days

期刊介绍： The mission of MCP is to foster the development and applications of proteomics in both basic and translational research. MCP will publish manuscripts that report significant new biological or clinical discoveries underpinned by proteomic observations across all kingdoms of life. Manuscripts must define the biological roles played by the proteins investigated or their mechanisms of action. The journal also emphasizes articles that describe innovative new computational methods and technological advancements that will enable future discoveries. Manuscripts describing such approaches do not have to include a solution to a biological problem, but must demonstrate that the technology works as described, is reproducible and is appropriate to uncover yet unknown protein/proteome function or properties using relevant model systems or publicly available data. Scope: -Fundamental studies in biology, including integrative "omics" studies, that provide mechanistic insights -Novel experimental and computational technologies -Proteogenomic data integration and analysis that enable greater understanding of physiology and disease processes -Pathway and network analyses of signaling that focus on the roles of post-translational modifications -Studies of proteome dynamics and quality controls, and their roles in disease -Studies of evolutionary processes effecting proteome dynamics, quality and regulation -Chemical proteomics, including mechanisms of drug action -Proteomics of the immune system and antigen presentation/recognition -Microbiome proteomics, host-microbe and host-pathogen interactions, and their roles in health and disease -Clinical and translational studies of human diseases -Metabolomics to understand functional connections between genes, proteins and phenotypes