Mps1 promotes chromosome meiotic chromosome biorientation through Dam1

Mol Biol Cell. 2018 Feb 15;29(4):479-489. doi: 10.1091/mbc.E17-08-0503. Epub 2017 Dec 13.

Abstract

In budding yeast meiosis, homologous chromosomes become linked by chiasmata and then move back and forth on the spindle until they are bioriented, with the kinetochores of the partners attached to microtubules from opposite spindle poles. Certain mutations in the conserved kinase, Mps1, result in catastrophic meiotic segregation errors but mild mitotic defects. We tested whether Dam1, a known substrate of Mps1, was necessary for its critical meiotic role. We found that kinetochore-microtubule attachments are established even when Dam1 is not phosphorylated by Mps1, but that Mps1 phosphorylation of Dam1 sustains those connections. But the meiotic defects when Dam1 is not phosphorylated are not nearly as catastrophic as when Mps1 is inactivated. The results demonstrate that one meiotic role of Mps1 is to stabilize connections that have been established between kinetochores and microtubles by phosphorylating Dam1.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Cell Cycle Proteins / genetics
  • Cell Cycle Proteins / metabolism
  • Cell Cycle Proteins / physiology*
  • Chromosome Segregation*
  • Kinetochores / enzymology
  • Meiosis*
  • Microtubule-Associated Proteins / genetics
  • Microtubule-Associated Proteins / physiology*
  • Microtubules / enzymology
  • Mutation
  • Phosphorylation
  • Protein Serine-Threonine Kinases / genetics
  • Protein Serine-Threonine Kinases / physiology*
  • Saccharomyces cerevisiae / enzymology
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / physiology*
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / physiology*
  • Spindle Apparatus / metabolism
  • Time-Lapse Imaging

Substances

  • Cell Cycle Proteins
  • DAM1 protein, S cerevisiae
  • Microtubule-Associated Proteins
  • Saccharomyces cerevisiae Proteins
  • Protein Serine-Threonine Kinases
  • MPS1 protein, S cerevisiae