Regulation of the subcellular shuttling of Sgo1 between centromeres and chromosome arms by Aurora B-mediated phosphorylation

Biochem Biophys Res Commun. 2014 Nov 21;454(3):429-35. doi: 10.1016/j.bbrc.2014.10.103. Epub 2014 Oct 28.

Abstract

A minor fraction of cohesin complexes at chromosome arms is not removed by the prophase pathway, and maintained until metaphase and enriched at centromeres. Sgo1 localizes to chromosome arms from prophase to metaphase, and is indispensable for removing cohesin complexes from chromosome arms. However, it has not been established how the chromosome arm localization of Sgo1 leads to the establishment of cohesion on chromosomes. Here, we report that Aurora B kinase interacts with and phosphorylates Sgo1 in vitro and in vivo. Furthermore, the phosphorylation of Sgol by Aurora B kinase regulated the distribution of Sgo1 between centromeres and chromosome arms, and the expression of Aurora B kinase-dead mutants of Sgo1 caused mislocalization from centromeres to chromosome arms. These results suggest Aurora B kinase directly regulates the subcellular distribution of Sgo1 to facilitate the accurate separation of mitotic chromosomes.

Keywords: Aurora B; Centromere; Chromosome arm; Phosphorylation; Sgo1; Sister chromatid cohesion.

MeSH terms

  • Aurora Kinase B / analysis
  • Aurora Kinase B / metabolism*
  • Cell Cycle Proteins / analysis
  • Cell Cycle Proteins / metabolism*
  • Centromere / metabolism*
  • Centromere / ultrastructure
  • Chromosome Segregation
  • HeLa Cells
  • Humans
  • Mitosis*
  • Phosphorylation

Substances

  • Cell Cycle Proteins
  • SGO1 protein, human
  • Aurora Kinase B