Arabidopsis 2010: Developing Paradigms for Functional Genomics of Protein Kinases and Phosphoproteins Using the CDPK Superfamily

摘要蛋白质磷酸化是真核细胞新陈代谢、基因表达和细胞结构的主要调控方式，确定基于磷酸化的调控网络对于了解拟南芥基因组的功能至关重要。这个项目的目标是定义与钙依赖蛋白激酶(CDPKs)功能相关的磷酸化网络以及四个密切相关的家族：CDPK相关蛋白(CRKs)、磷酸烯醇式丙酮酸羧化酶(PPCKs)、PPCK相关蛋白(PEPRKs)和SNF-1相关蛋白(SnRKs)。这88个蛋白激酶约占拟南芥基因组中所有蛋白激酶的9%，参与植物发育和生理的各个方面，并参与细胞对环境信号和发育信号的反应。包括基因识别号在内的这些蛋白激酶的列表可在http://www.arabidopsis.org，上获得，包括数据库记录链接在内的进一步信息可在http://plantsp.sdsc.edu.上获得。本研究将通过确定每个激酶的亚细胞位置以及确定下游靶标和其他与这些激酶相关的蛋白来研究这些家族成员的功能。这些信息将通过识别每个激酶参与的信号网络来深入了解每个激酶的生理作用。这项研究还将确定底物蛋白中被每一种蛋白磷酸化的靶序列，这些结果将有助于理解蛋白激酶功能的重叠和信号通路之间的串扰。这项工作的结果将每年在上述两个网址上公布。

Abstract Protein phosphorylation is a major mode of regulation of metabolism, gene expression, and cellular architecture in eukaryotic cells, and defining phosphorylation-based regulatory networks is essential for understanding the function of the Arabidopsis genome. The goal of this project is to define phosphorylation networks that are related to the function of calcium-dependent protein kinases (CDPKs) and four closely related families; CDPK-related kinases (CRKs), phosphoenolpyruvate carboxylase kinases (PPCKs), PPCK-related kinases (PEPRKs), and SNF-1 related kinases (SnRKs). These 88 kinases, which represent about 9% of all the protein kinases in the Arabidopsis genome, are involved in all aspects of plant development and physiology and participate in the coupling of cellular responses to environmental and developmental signals. A list of these protein kinases including gene identification numbers is available at http://www.arabidopsis.org, and further information including links to database records is available at http://plantsp.sdsc.edu. This research will investigate the function of 64 members of these families through determination of the subcellular location of each kinase and identification of downstream targets and other proteins with which the kinases associate. This information will give insight into the physiological roles of each kinase by identifying signaling networks in which each participates. This research will also determine the target sequences in substrate proteins that are phosphorylated by each kinase, and these results will contribute to understanding the overlap in kinase function and cross-talk between signaling pathways. The results of this work will be made available on a yearly basis at the two URLs given above.