Signaling pathways involved in the phosphorylation of membrane proteins in response to N and C

参与响应 N 和 C 的膜蛋白磷酸化的信号通路

基本信息

批准号：
242598629
负责人：
Professorin Dr. Waltraud Schulze
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：
2013
资助国家：
德国
起止时间：
2012-12-31 至 2017-12-31
项目状态：
已结题

来源：
https://gepris.dfg.de/gepris/projekt/242598629?language=en
关键词：
Signaling pathways involved phosphorylation membrane

项目摘要

Nitrogen is an essential macronutrient for plant growth. In addition, nitrogen also has signaling functions by triggering specific adaptations in central metabolism and root development. While basic uptake mechanisms for nitrate through plasma membrane located transport systems are well known and global transcriptional responses to changes in nitrogen availability have been studied in the past, the detailed mechanisms in regulation of nitrate uptake, as well as signal transduction events upstream of transcription are still barely revealed. Our work will aim at closing this gap by particularly focusing on studying the regulation of nitrate transporter NRT2.1 and nitrate responsive protein kinases. Phosphorylation is the most well studied post-translational modification with regulatory function. It can induce changes in protein activity, provide docking sites for protein-protein interaction or induce changes in subcellular location. Nitrate transporters were in the past shown to be subject to protein phosphorylation, and especially for NRT1.1 the role of protein phosphorylation in switching of transport affinity has been well described. Also for ammonium transporters, a phosphorylation-dependent activation/inactivation mechanism was elucidated in recent years. Therefore, a particular focus of this project is to study the role of protein phosphorylation for the regulation of the major nitrate transporter NRT2.1.Within the last couple of years, the general picture has emerged that both NO3- and NH4+ transporters are controlled at the protein level by posttranslational modification to ensure fast responses directly at the plasma membrane to highly fluctuating environmental conditions. Therefore, the scientific aim of this collaborative project is (i) to characterize the condition-dependent phosphorylation of target proteins related to N metabolism in response to C and N availability. It will involve both the identification novel C/N regulated proteins as well as the specific characterisation of the role of the known NRT2.1 phosphorylation sites. The project aim at (ii) finding candidate protein kinases and/or phosphatases using both NRT2.1 and selected nitrogen-metabolism related proteins as targets and (iii) characterising in vivo the impact of the interesting protein kinases and/or phosphatases on the phosphorylation of NRT2.1 and selected nitrogen metabolism related proteins. We will also start to investigate the proteins interacting with the selected protein kinases and/or phosphatases as baits. We are convinced that with the complementary expertise of both partner groups and with a clear focus on NRT2.1 regulation on protein level, we will gain novel valuable insights into a crucial plant function, namely the regulation of nitrogen uptake.

氮是植物生长的必需大量营养素。此外，氮还通过触发中央代谢和根发育中的特定适应性来具有信号传导功能。虽然过去已经研究了通过质膜的基本摄取机制通过质膜定位的运输系统，并且过去已经研究了对氮利用率变化的全球转录响应，但调节硝酸盐吸收的详细机制，以及转录上游上游的信号转导事件的调节。我们的工作将旨在通过研究硝酸盐转运蛋白NRT2.1和硝酸盐反应性蛋白激酶的调节来缩小这一差距。磷酸化是通过调节功能进行的翻译后修饰最精心良好的。它可以诱导蛋白质活性的变化，为蛋白质蛋白质相互作用提供对接位点，或诱导亚细胞位置的变化。硝酸盐转运蛋白过去被证明受到蛋白质磷酸化的影响，尤其是对于NRT1.1，蛋白质磷酸化在转运亲和力切换中的作用已得到很好的描述。同样对于铵转运蛋白，近年来阐明了磷酸化依赖性激活/灭活机制。因此，该项目的一个特殊重点是研究蛋白质磷酸化对主要硝酸盐转运蛋白转运蛋白NRT2.1的作用。在过去的几年中，一般的情况已经出现，已经出现了NO3-和NH4+转运蛋白在蛋白质水平上在蛋白质水平上通过plastification pation Factifation在plasmakation plassifation plasemation plassmagation plassmakation the Plassmbrane flas flauta flaunation plass embrane folbrane fol.membrane flauth embrrane flauth embrrane fol.Membrbrane flau embrrane fol.因此，该协作项目的科学目的是（i）表征与n代谢相关的靶蛋白的条件依赖性磷酸化，以响应C和N的可用性。它将涉及鉴定新型C/N调节蛋白以及已知NRT2.1磷酸化位点的作用的特定表征。该项目的目的是（ii）使用NRT2.1并选择氮与代谢相关的蛋白质作为靶标，并且（iii）在体内表征有趣的蛋白激酶和/或磷酸酶对NRT2.1磷酸化对NRT2.1和选择氮的蛋白质的影响。我们还将开始研究与所选蛋白激酶和/或磷酸酶作为诱饵相互作用的蛋白质。我们坚信，借助两个伙伴群体的互补专业知识，并明确着眼于NRT2.1对蛋白质水平的调节，我们将获得对关键植物功能的新颖有价值的见解，即对氮摄取的调节。