KINETOCHORE PROTEIN INTERACTIONS AND THEIR REGULATORY KINASES

动粒蛋白相互作用及其调节激酶

• 批准号: 8171310
• 负责人: DAVID G DRUBIN
• 金额: $ 0.24万
• 依托单位: UNIVERSITY OF WASHINGTON
• 依托单位国家: 美国
• 财政年份: 2010
• 资助国家: 美国
• 起止时间: 2010-09-01 至 2011-08-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8171310
• 关键词: Computer Retrieval of Information on Scientific Projects Database; DNA; Funding; Grant; Institution; Kinetochores; Maps; Mass Spectrum Analysis; Microtubules; Mitotic; Mitotic spindle; Modification; Mutate; Phosphorylation; Phosphorylation Site; Phosphotransferases; Proteins; Regulation; Research; Research Personnel; Resources; Saccharomycetales; Site; Source; United States National Institutes of Health; in vivo; insight

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. The budding yeast kinetochore connects spindle microtubules to centromeric DNA and is critical in mitotic spindle function. A number of kinetochore proteins are phosphorylated by mitotic kinases but what impact these modifications have on their regulation has yet to be understood. Here we use mass spectrometry to map sites of phosphorylation, as well as in vivo studies, in order to understand the functional consequences of mutating these sites. This will allow us to gain more insight into the impact of phosphorylation on kinetochore protein interactions and the regulation of the mitotic spindle and budding yeast kinetochore.

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 芽殖酵母动粒连接纺锤体微管和着丝粒DNA，在有丝分裂纺锤体功能中至关重要。许多动粒蛋白被有丝分裂激酶磷酸化，但这些修饰对它们的调节有什么影响还有待了解。 在这里，我们使用质谱来定位磷酸化位点，以及体内研究，以了解这些位点突变的功能后果。这将使我们能够更深入地了解磷酸化对动粒蛋白相互作用的影响以及有丝分裂纺锤体和芽殖酵母动粒的调节。