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

J Biol Chem. 2009 Jul 10;284(28):18692-8. doi: 10.1074/jbc.M109.012732. Epub 2009 Apr 27.

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 Ser(361) on Sgt1, and this phosphorylation inhibits Sgt1 dimerization.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Signal Transducing / chemistry
  • Adaptor Proteins, Signal Transducing / physiology*
  • Amino Acid Sequence
  • Casein Kinase II / chemistry*
  • HSP90 Heat-Shock Proteins / chemistry
  • HSP90 Heat-Shock Proteins / physiology*
  • Humans
  • Kinetochores / chemistry
  • Molecular Sequence Data
  • Nuclear Proteins / chemistry
  • Phosphorylation
  • Plasmids / metabolism
  • Protein Binding
  • Protein Multimerization
  • Saccharomyces cerevisiae / metabolism
  • Saccharomyces cerevisiae Proteins / chemistry
  • Saccharomyces cerevisiae Proteins / physiology*
  • Serine / chemistry
  • Time Factors

Substances

  • Adaptor Proteins, Signal Transducing
  • CTF13 protein, S cerevisiae
  • HSP82 protein, S cerevisiae
  • HSP90 Heat-Shock Proteins
  • Nuclear Proteins
  • SGT1 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Serine
  • Casein Kinase II