Nono, a Bivalent Domain Factor, Regulates Erk Signaling and Mouse Embryonic Stem Cell Pluripotency

Cell Rep. 2016 Oct 18;17(4):997-1007. doi: 10.1016/j.celrep.2016.09.078.

Abstract

Nono is a component of the para-speckle, which stores and processes RNA. Mouse embryonic stem cells (mESCs) lack para-speckles, leaving the function of Nono in mESCs unclear. Here, we find that Nono functions as a chromatin regulator cooperating with Erk to regulate mESC pluripotency. We report that Nono loss results in robust self-renewing mESCs with epigenomic and transcriptomic features resembling the 2i (GSK and Erk inhibitors)-induced "ground state." Erk interacts with and is required for Nono localization to a subset of bivalent genes that have high levels of poised RNA polymerase. Nono loss compromises Erk activation and RNA polymerase poising at its target bivalent genes in undifferentiated mESCs, thus disrupting target gene activation and differentiation. These findings argue that Nono collaborates with Erk signaling to regulate the integrity of bivalent domains and mESC pluripotency.

Keywords: Erk; Neat1; Nono; RNAPII; bivalent domain; ground state; mESC; p54NRB; para-speckle; pluripotency.

MeSH terms

  • Animals
  • Cell Differentiation / genetics
  • Cell Self Renewal
  • DNA-Binding Proteins / metabolism*
  • Enzyme Activation
  • Epigenesis, Genetic
  • Gene Expression Profiling
  • Genome
  • Kruppel-Like Factor 4
  • Kruppel-Like Transcription Factors / metabolism
  • MAP Kinase Signaling System*
  • Mice
  • Mice, Knockout
  • Mouse Embryonic Stem Cells / cytology
  • Mouse Embryonic Stem Cells / metabolism*
  • Nanog Homeobox Protein / metabolism
  • Phosphorylation
  • Pluripotent Stem Cells / cytology*
  • Pluripotent Stem Cells / metabolism*
  • RNA-Binding Proteins
  • Transcriptome / genetics

Substances

  • DNA-Binding Proteins
  • Kruppel-Like Factor 4
  • Kruppel-Like Transcription Factors
  • Nanog Homeobox Protein
  • Nono protein, mouse
  • RNA-Binding Proteins