POSTTRANSLATIONAL MODIFICATIONS OF CYTOKERATIN PROTEINS

细胞角蛋白的翻译后修饰

• 批准号: 7369023
• 负责人: ALMA L BURLINGAME
• 金额: --
• 依托单位: UNIVERSITY OF CALIFORNIA, SAN FRANCISCO
• 依托单位国家: 美国
• 财政年份: 2006
• 资助国家: 美国
• 起止时间: 2006-03-01 至 2007-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7369023
• 关键词: POSTTRANSLATIONAL; MODIFICATIONS; CYTOKERATIN; PROTEINS

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Our goal is to determine phosphorylation and O-linked glycosylation sites on cytokeratin polypeptide 8, studying cytokeratin polypeptide 8 and possibly cytokeratin polypeptide 18 at the mass spectrometry level. We hope to obtain detailed structural information to support our initial biochemical data indicating that this cytokeratin has a single N-acetylglucosamine residue we presume is linked to serine. We also hope our system coupled with mass spectrometry would determine if there is an inverse relationship between the state of serine phosphorylation and O-linked glycosylation. Cytokeratin proteins make up an ideal system to study this question since they are heavily phosphorylated on serine residues and in addition have the O-linked glycosylation and are present in cells in large quantities, making them amenable for mass spec sequencing studies. A variety of methods are being pursued aimed at development of a robust mass spectrometric strategy for the site specific characterization of O-GlcNAc residues on nuclear proteins for comparison with phosphorylation sites on the same proteins.. 293C

这个子项目是利用由NIH/NCRR资助的中心拨款提供的资源的许多研究子项目之一。子项目和调查员(PI)可能从另一个NIH来源获得了主要资金，因此可能会出现在其他CRISE条目中。列出的机构是针对中心的，而不一定是针对调查员的机构。我们的目标是确定细胞角蛋白多肽8上的磷酸化和O连接的糖基化位点，在质谱学水平上研究细胞角蛋白多肽8和可能的细胞角蛋白多肽18。我们希望获得详细的结构信息来支持我们最初的生化数据，表明这种细胞角蛋白含有一个N-乙酰氨基葡萄糖残基，我们推测它与丝氨酸有关。我们还希望我们的系统与质谱学相结合，能够确定丝氨酸磷酸化状态和O-连接糖基化状态之间是否存在反向关系。细胞角蛋白蛋白是研究这一问题的理想系统，因为它们在丝氨酸残基上高度磷酸化，并且具有O-连接的糖基化作用，并且大量存在于细胞中，使它们适合于质谱仪测序研究。人们正在寻求各种方法，目的是开发一种强有力的质谱学策略，用于核蛋白上O-GlcNAc残基的特定位点表征，以便与相同蛋白质上的磷酸化位点进行比较。293C