Tex19.1 inhibits the N-end rule pathway and maintains acetylated SMC3 cohesin and sister chromatid cohesion in oocytes

J Cell Biol. 2020 May 4;219(5):e201702123. doi: 10.1083/jcb.201702123.

Abstract

Age-dependent oocyte aneuploidy, a major cause of Down syndrome, is associated with declining sister chromatid cohesion in postnatal oocytes. Here we show that cohesion in postnatal mouse oocytes is regulated by Tex19.1. We show Tex19.1-/- oocytes have defects maintaining chiasmata, missegregate their chromosomes during meiosis, and transmit aneuploidies to the next generation. Furthermore, we show that mouse Tex19.1 inhibits N-end rule protein degradation mediated by its interacting partner UBR2, and that Ubr2 itself has a previously undescribed role in negatively regulating the acetylated SMC3 subpopulation of cohesin in mitotic somatic cells. Lastly, we show that acetylated SMC3 is associated with meiotic chromosome axes in mouse oocytes, and that this population of cohesin is specifically depleted in the absence of Tex19.1. These findings indicate that Tex19.1 regulates UBR protein activity to maintain acetylated SMC3 and sister chromatid cohesion in postnatal oocytes and prevent aneuploidy from arising in the female germline.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aneuploidy
  • Animals
  • Cell Cycle Proteins / genetics*
  • Cell Lineage / genetics
  • Chondroitin Sulfate Proteoglycans / genetics*
  • Chromatids / genetics
  • Chromosomal Proteins, Non-Histone / genetics*
  • Chromosome Segregation / genetics
  • Cohesins
  • Female
  • Germ Cells / growth & development
  • Humans
  • Meiosis / genetics
  • Mice
  • Mice, Knockout
  • Oocytes / growth & development
  • Oocytes / metabolism
  • RNA-Binding Proteins / genetics*
  • Sister Chromatid Exchange / genetics*
  • Ubiquitin-Protein Ligases / genetics*

Substances

  • Cell Cycle Proteins
  • Chondroitin Sulfate Proteoglycans
  • Chromosomal Proteins, Non-Histone
  • Cspg6 protein, mouse
  • RNA-Binding Proteins
  • Tex19 protein, mouse
  • UBR2 protein, mouse
  • Ubiquitin-Protein Ligases