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

质膜是细胞质溶胶与外界环境之间物质（营养物质、激素）交换的边界室。植物必须根据环境的变化迅速调整细胞状态、生长发育和代谢。近年来，越来越多的证据表明，质膜的蛋白质组成具有高度的动态性和刺激依赖性。在植物的质膜中，H+- atp酶是含量最多的蛋白质。H+- atp酶不仅是跨膜溶质运输所必需的，而且还可以影响细胞的伸长、气孔的打开和关闭以及对环境胁迫和病原体攻击的反应。因此，H+- atp酶受到高度调控，特别是通过不同激酶在几个激活和抑制位点的磷酸化。最近在质膜内发现了短而直接的调节途径，包括受体激酶调节质子泵、水通道和其他膜转运蛋白，这表明这是一个模块化的通用原理，允许植物非常迅速地适应变化和具有挑战性的环境。我们提出，依赖于外部条件，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分，导致有条件的相互作用和H+- atp酶在激活或抑制磷酸化位点的磷酸化。基于提出的质膜内动态功能蛋白复合物模型，我们旨在利用蛋白质组学和现代光谱显微镜方法相结合，系统地研究质膜H+- atp酶AHA2如何在外界刺激下形成不同的蛋白质复合物。因此，我们对动态招募到这些AHA2功能复合物中的受体激酶/共受体对特别感兴趣

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