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.

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