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

质膜是细胞质与外部环境之间物质（营养物质、激素）交换的边界区室。植物必须快速调整其细胞状态、生长发育和新陈代谢以适应环境的变化。近年来，越来越明显的是质膜的蛋白质组成是高度动态的和刺激依赖性的。在植物质膜内，H+-ATP酶是最丰富的蛋白质。 H+-ATP酶不仅对于跨膜溶质转运至关重要，而且还可以影响细胞伸长、气孔的打开和关闭以及对环境应激和病原体攻击的反应。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。最近发现质膜内涉及调节质子泵、水通道和其他膜转运蛋白的受体激酶的短而直接的调节途径表明，这是一种模块化的通用原理，允许植物非常快速地适应不断变化和具有挑战性的环境。我们认为，根据外部条件，与 H+-ATP 酶相互作用的受体/辅助受体对是动态复合物的可变组成部分，导致 H+-ATP 酶在激活或抑制磷酸化位点处发生条件性相互作用和磷酸化。为了研究质膜内的动态功能蛋白复合物，我们的目标是结合蛋白质组学和现代技术，系统地研究质膜 H+-ATPase AHA2 如何根据外部刺激形成不同的蛋白复合物。光谱显微镜方法。因此，我们对动态招募到 AHA2 功能复合物中的受体激酶/共受体对特别感兴趣

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）

Comparison of path-based centrality measures in protein-protein interaction networks revealed proteins with phenotypic relevance during adaptation to changing nitrogen environments.

蛋白质-蛋白质相互作用网络中基于路径的中心性测量的比较揭示了蛋白质在适应不断变化的氮环境过程中具有表型相关性。

DOI：
10.1016/j.jprot.2021.104114
发表时间：
2021-01-13
期刊：
Journal of proteomics
影响因子：
0
作者：
Max Gilbert;Zhi Li;X. Wu;Le;er Rohr;er;Sven Gombos;K. Harter;W. Schulze
通讯作者：
W. Schulze

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

三荧光团 FRET-FLIM 能够以纳米级分辨率研究活植物细胞中的三聚体蛋白质相互作用和复合物形成

DOI：
10.1101/722124
发表时间：
2019-08-01
期刊：
bioRxiv
影响因子：
0
作者：
Nina Gloeckner;S. Z. Oven;F. Wackenhut;Moritz Burmeister;Friederike Wanke;E. Holzwart;A.
通讯作者：
A.

Global Identification of Protein Complexes within the Membrane Proteome of Arabidopsis Roots Using a SEC-MS Approach.

使用 SEC-MS 方法全面鉴定拟南芥根膜蛋白质组中的蛋白质复合物