DECIPHERING THE PHOSPHOPROTEOME OF T LYMPHOCYTES

破译 T 淋巴细胞的磷酸蛋白质组

• 批准号: 8363775
• 负责人: ALMA L BURLINGAME
• 金额: $ 0.13万
• 依托单位: UNIVERSITY OF CALIFORNIA, SAN FRANCISCO
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-06-01 至 2012-05-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8363775
• 关键词: Apoptosis; Cell Cycle; Cell physiology; Cells; Event; Funding; Grant; Human; Immune response; Lymphocyte; Mass Spectrum Analysis; Mediating; Methods; National Center for Research Resources; Phosphorylated Peptide; Phosphorylation; Play; Post-Translational Protein Processing; Principal Investigator; Protein Dephosphorylation; Proteins; Proteomics; Research; Research Infrastructure; Resources; Role; Signal Transduction; Site; Source; T-Lymphocyte; United States National Institutes of Health; cost; response

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. Phosphorylation is one of the most frequent posttranslational modifications of proteins. In a cell, about 30% of the total proteins are phosphorylated to some extent. Protein phosphorlyation-dephosphorylation events play a primary role in almost all aspects of cell function including signal transduction, cell cycle or apoptosis. The activation of the immune response mediated by T lymphocytes is dependent on protein phosphorylation-dephosphorylation events. In order to understand the functionality of lymphocytes in an immune response we need to study the phosphorylation profiles that occur in these cells in response to activation. Considering the complexity of a whole cell lysate and the low amount of phosphorylated peptides versus the non-phosphorylated ones, a robust and effective method for the analysis of the phosphoproteome is of the highest importance in the field of proteomics. Mass spectrometry will be used to identify different posttranslational modifications, such as phosphorylation and their site assignment in human primary T cells. Quantitative methods, such as iTRAQ, will be used to determine the dynamics of the phosphorylation state.

这个子项目是利用资源的许多研究子项目之一。 由NIH/NCRR资助的中心拨款提供。对子项目的主要支持 子项目的首席调查员可能是由其他来源提供的， 包括美国国立卫生研究院的其他来源。为子项目列出的总成本可能 表示该子项目使用的中心基础设施的估计数量， 不是由NCRR赠款提供给次级项目或次级项目工作人员的直接资金。 磷酸化是蛋白质最常见的翻译后修饰之一。在细胞中，大约30%的总蛋白质在某种程度上被磷酸化。蛋白质磷酸化-去磷酸化事件在细胞功能的几乎所有方面都发挥着重要作用，包括信号转导、细胞周期或细胞凋亡。T淋巴细胞介导的免疫反应的激活依赖于蛋白质磷酸化-去磷酸化事件。为了了解淋巴细胞在免疫反应中的功能，我们需要研究这些细胞在激活时发生的磷酸化情况。考虑到整个细胞裂解产物的复杂性以及与非磷酸化多肽相比，磷酸化多肽的数量较少，因此一种稳健而有效的分析磷酸蛋白质组的方法在蛋白质组学领域具有非常重要的意义。质谱学将被用来识别不同的翻译后修饰，如磷酸化及其在人类原始T细胞中的位置分配。定量方法，如iTRAQ，将被用来确定磷酸化状态的动力学。