STU1P FUNCTION IN BUDDING YEAST MITOSIS

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的研究机构。 Stu 1 p是酿酒酵母中一种必需的微管结合蛋白，其功能是调节有丝分裂纺锤体结构。它是后生动物中微管加末端跟踪蛋白CLASP家族的同系物。CLASP家族的结合伴侣已经在后生动物中被确定，但Stu 1 p的结合伴侣是未知的。我们正试图确定Stu 1 p是否与其他参与有丝分裂的蛋白质相互作用，特别是在有丝分裂纺锤体完整性方面。Stu 1 p也是一种磷酸化蛋白，但使其磷酸化的激酶尚不清楚。我们正试图确定Stu 1 p的所有磷酸化残基，以及确定负责这种磷酸化的激酶，以及磷酸化是否是Stu 1 p功能的调节剂。

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.