STU1P FUNCTION IN BUDDING YEAST MITOSIS

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。 Stu1p是酿酒酵母中必需的微管结合蛋白，是有丝分裂纺锤体结构的调节因子。它是后生动物中微管加末端跟踪蛋白的CLASP家族的同源物。在后生动物中已经发现了CLASP家族的结合伙伴，但Stu1p的结合伙伴尚不清楚。我们正试图确定Stu1p是否与参与有丝分裂的其他蛋白质相互作用，特别是有丝分裂纺锤体的完整性。Stu1p也是一种磷酸化蛋白，但使其磷酸化的激酶(S)尚不清楚。我们正试图鉴定Stu1p的所有磷酸化残基，并确定负责这种磷酸化的激酶以及磷酸化是否是Stu1p功能的调节因子。

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. Stu1p is an essential microtubule-binding protein in Saccharomyces cerevisiae, and functions as a regulator of mitotic spindle structure. It is a homolog of the CLASP family of microtubule plus end tracking proteins in metazoans. CLASP family binding partners have been identified in metazoans, but Stu1p's binding partners are unknown. We are trying to determine if Stu1p interacts with other proteins involved in mitosis, particularly in mitotic spindle integrity. Stu1p is also a phospho-protein, but the kinase(s) that phosphorylate it are unknown. We are attempting to identify all phosphorylated residues of Stu1p, as well as determine the kinases responsible for this phosphorylation and if phosphorylation is a regulator of Stu1p function.