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.

该副本是利用众多研究子项目之一 由NIH/NCRR资助的中心赠款提供的资源。子弹和 调查员（PI）可能已经从其他NIH来源获得了主要资金， 因此可以在其他清晰的条目中代表。列出的机构是 对于中心，这不一定是调查员的机构。 萌芽的酵母动力学将纺锤体微管连接到丝粒DNA，在有丝分裂纺锤体功能中至关重要。许多动力学蛋白被有丝分裂激酶磷酸化，但是这些修饰对它们的调节的影响尚待了解。 在这里，我们使用质谱法来绘制磷酸化的位点以及体内研究，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力学蛋白相互作用的影响以及有丝分裂纺锤体和发芽的酵母菌的调节。