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利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 发芽酵母着丝粒连接纺锤体微管和着丝粒DNA，在有丝分裂纺锤体功能中起关键作用。许多动粒蛋白被有丝分裂酶磷酸化，但这些修饰对它们的调节有什么影响还不清楚。在这里，我们使用质谱学来绘制磷酸化位点的图谱，以及体内研究，以了解突变这些位点的功能后果。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发芽酵母动粒的调节。