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

J Biol Chem

Department of Molecular Pharmacology, Hartwell Center for Bioinformatics and Biotechnology, St. Jude Children's Research Hospital, Memphis, Tennessee 38105-3678, USA.

Published: July 2009

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.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2707205PMC
http://dx.doi.org/10.1074/jbc.M109.012732DOI Listing

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