Bansal Parmil K, Mishra Ashutosh, High Anthony A, Abdulle Rashid, Kitagawa Katsumi
Department of Molecular Pharmacology, Hartwell Center for Bioinformatics and Biotechnology, St. Jude Children's Research Hospital, Memphis, Tennessee 38105-3678, USA.
J Biol Chem. 2009 Jul 10;284(28):18692-8. doi: 10.1074/jbc.M109.012732. Epub 2009 Apr 27.
The kinetochore, which consists of centromere DNA and structural proteins, is essential for proper chromosome segregation in eukaryotes. In budding yeast, Sgt1 and Hsp90 are required for the binding of Skp1 to Ctf13 (a component of the core kinetochore complex CBF3) and therefore for the assembly of CBF3. We have previously shown that Sgt1 dimerization is important for this kinetochore assembly mechanism. In this study, we report that protein kinase CK2 phosphorylates Ser(361) on Sgt1, and this phosphorylation inhibits Sgt1 dimerization.
动粒由着丝粒DNA和结构蛋白组成,对真核生物中染色体的正确分离至关重要。在芽殖酵母中,Sgt1和Hsp90是Skp1与Ctf13(核心动粒复合体CBF3的一个组分)结合所必需的,因此也是CBF3组装所必需的。我们之前已经表明,Sgt1二聚化对这种动粒组装机制很重要。在本研究中,我们报告蛋白激酶CK2使Sgt1上的Ser(361)磷酸化,这种磷酸化抑制Sgt1二聚化。