Sgt1 Dimerization Is Negatively Regulated by Protein Kinase CK2-mediated Phosphorylation at Ser361
Sgt1 Dimerization Is Negatively Regulated by Protein Kinase CK2-mediated Phosphorylation at Ser361
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DOI：
10.1074/jbc.m109.012732
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发表时间：
2009-07-10
影响因子：
4.8
通讯作者：
Kitagawa, Katsumi
中科院分区：
文献类型：
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作者：
Bansal, Parmil K.;Mishra, Ashutosh;Kitagawa, Katsumi
动粒由着丝粒DNA和结构蛋白组成，是真核生物染色体正确分离所必需的。在芽殖酵母中，Sgt1和Hsp90是Skp1与Ctf13（核心动粒复合物CBF3的一种组分）结合所必需的，因此也是CBF3组装所必需的。我们以前已经表明，Sgt1二聚化是重要的动粒组装机制。在这项研究中，我们报告了蛋白激酶CK2磷酸化Sgt1上的Ser（361），这种磷酸化抑制了Sgt1的二聚化。
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.