Sgt1 dimerization is negatively regulated by protein kinase CK2-mediated phosphorylation at Ser361

Parkil K. Bansal; Ashutosh Mishra; Anthony A. High; Rashid Abdelle; Katsumi Kitagawa

doi:10.1074/jbc.M109.012732

Sgt1 dimerization is negatively regulated by protein kinase CK2-mediated phosphorylation at Ser³⁶¹

Parkil K. Bansal, Ashutosh Mishra, Anthony A. High, Rashid Abdelle, Katsumi Kitagawa

Molecular Medicine

Research output: Contribution to journal › Article

20 Scopus citations

Abstract

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 Ser³⁶¹ on Sgt1, and this phosphorylation inhibits Sgt1 dimerization.

Original language	English (US)
Pages (from-to)	18692-18698
Number of pages	7
Journal	Journal of Biological Chemistry
Volume	284
Issue number	28
DOIs	https://doi.org/10.1074/jbc.M109.012732
State	Published - Jul 10 2009

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ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

Cite this

Bansal, P. K., Mishra, A., High, A. A., Abdelle, R., & Kitagawa, K. (2009). Sgt1 dimerization is negatively regulated by protein kinase CK2-mediated phosphorylation at Ser³⁶¹. Journal of Biological Chemistry, 284(28), 18692-18698. https://doi.org/10.1074/jbc.M109.012732

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10.1074/jbc.M109.012732