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Dynamics of functional membrane complexes associated with the plasma membrane H+-ATPase AHA2

与质膜 H-ATP 酶 AHA2 相关的功能性膜复合物的动力学

基本信息

批准号：
327797394
负责人：
Professor Dr. Klaus Harter
金额：
--
依托单位：
Fachgebiet Systembiologie der Pflanze (190d)
依托单位国家：
德国
项目类别：
Research Grants
财政年份：
2017
资助国家：
德国
起止时间：
2016-12-31 至 2020-12-31
项目状态：
已结题

来源：
https://gepris.dfg.de/gepris/projekt/327797394?language=en
关键词：
Dynamics functional membrane complexes associated

项目摘要

The plasma membrane is the boundary compartment which enables exchange of substances (nutrients, hormones) between cytosol and the outside environment. Plants must rapidly adjust their cellular status, growth and development and metabolism to changes in the environment. In recent years it became more and more evident that the protein composition of the plasma membrane is highly dynamic and stimulus-dependent. Within the plasma membrane of plants, the H+-ATPases are the most abundant proteins. The H+-ATPases are not only essential for transmembrane solute transport, but can also affect cell elongation, the opening and closing of the stomata and the responses to environmental stress and pathogen attack. Thus, the H+-ATPases are highly regulated, particularly by phosphorylation at several activating and inhibiting sites by different kinases. The recent discovery of short, direct regulatory pathways within the plasma membrane involving receptor kinases regulating proton pumps, water channels and other membrane transporters suggests that this is a modular generic principle allowing plants to very rapidly adjust to changing and challenging environments. We propose that dependent on external conditions, the receptor/coreceptor pairs interacting with the H+-ATPase are variable components of a dynamic complex resulting in conditional interactions and phosphorylation of the H+-ATPase at activating or inhibiting phosphorylation sites.Based on the proposed model of dynamic functional protein complexes within the plasma membrane, we aim at systematically studying how the plasma membrane H+-ATPase AHA2 forms different protein complexes dependent on external stimuli using a combination of proteomics and modern spectro-microscopic methods. Thereby, we are particularly interested in the receptor kinase / co-receptor pairs dynamically recruited into these functional complexes of AHA2

质膜是细胞质和外界环境之间物质（营养物质、激素）交换的边界区室。植物必须迅速调整其细胞状态，生长发育和代谢以适应环境的变化。近年来，越来越多的证据表明，质膜的蛋白质组成是高度动态和刺激依赖性的。在植物的质膜内，H+-ATP酶是最丰富的蛋白质。H ~+-ATP酶不仅参与跨膜溶质运输，而且还影响细胞的伸长、气孔的开闭以及对环境胁迫和病原菌侵袭的反应。因此，H+-ATP酶受到高度调节，特别是通过不同激酶在几个激活和抑制位点的磷酸化。最近发现的短，直接的调节途径，质膜内涉及受体激酶调节质子泵，水通道和其他膜转运蛋白表明，这是一个模块化的一般原则，使植物非常迅速地适应不断变化的和具有挑战性的环境。我们认为，依赖于外界条件，与H ~+-ATP酶相互作用的受体/辅助受体对是一个动态复合物的可变组分，导致条件相互作用和H ~+-ATP酶在激活或抑制磷酸化位点的磷酸化。本研究旨在利用蛋白质组学和现代光谱显微镜相结合的方法，系统地研究质膜H+-ATPase AHA 2如何依赖于外界刺激形成不同的蛋白质复合物。因此，我们特别感兴趣的是受体激酶/共受体对动态招募到这些功能复合物的AHA 2

项目成果

期刊论文数量（4）

专著数量（0）

科研奖励数量（0）

会议论文数量（0）

专利数量（0）

Quantitative description & computational modelling of the BRI1 response module controlling root cell elongation growth – from organ-scale to nanodomains

定量描述

DOI：
10.15496/publikation-35158
发表时间：
2019
期刊：
影响因子：
0
作者：
Glöckner
通讯作者：
Glöckner

Three-fluorophore FRET-FLIM enables the study of trimeric protein interactions and complex formation with nanoscale resolution in living plant cells

DOI：
10.1101/722124
发表时间：
2019-08
期刊：
bioRxiv
影响因子：
0
作者：
Nina Gloeckner;S. Z. Oven-Krockhaus;F. Wackenhut;Moritz Burmeister;Friederike Wanke;E. Holzwart;
通讯作者：
Nina Gloeckner;S. Z. Oven-Krockhaus;F. Wackenhut;Moritz Burmeister;Friederike Wanke;E. Holzwart;