Laminopathies disrupt epigenomic developmental programs and cell fate

Sci Transl Med. 2016 Apr 20;8(335):335ra58. doi: 10.1126/scitranslmed.aad4991.

Abstract

The nuclear envelope protein lamin A is encoded by thelamin A/C(LMNA) gene, which can contain missense mutations that cause Emery-Dreifuss muscular dystrophy (EDMD) (p.R453W). We fused mutated forms of the lamin A protein to bacterial DNA adenine methyltransferase (Dam) to define euchromatic-heterochromatin (epigenomic) transitions at the nuclear envelope during myogenesis (using DamID-seq). Lamin A missense mutations disrupted appropriate formation of lamin A-associated heterochromatin domains in an allele-specific manner-findings that were confirmed by chromatin immunoprecipitation-DNA sequencing (ChIP-seq) in murine H2K cells and DNA methylation studies in fibroblasts from muscular dystrophy patient who carried a distinctLMNAmutation (p.H222P). Observed perturbations of the epigenomic transitions included exit from pluripotency and cell cycle programs [euchromatin (open, transcribed) to heterochromatin (closed, silent)], as well as induction of myogenic loci (heterochromatin to euchromatin). In muscle biopsies from patients with either a gain- or change-of-functionLMNAgene mutation or a loss-of-function mutation in theemeringene, both of which cause EDMD, we observed inappropriate loss of heterochromatin formation at theSox2pluripotency locus, which was associated with persistent mRNA expression ofSox2 Overexpression ofSox2inhibited myogenic differentiation in human immortalized myoblasts. Our findings suggest that nuclear envelopathies are disorders of developmental epigenetic programming that result from altered formation of lamina-associated domains.

Publication types

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

MeSH terms

  • Animals
  • Cell Cycle / genetics
  • Cell Cycle / physiology
  • Cell Differentiation / genetics
  • Cell Differentiation / physiology
  • Cell Nucleus / genetics
  • Cell Nucleus / metabolism
  • Cells, Cultured
  • Chromatin Immunoprecipitation
  • Computational Biology
  • DNA Methylation / genetics
  • DNA Methylation / physiology
  • Epigenesis, Genetic / genetics*
  • HEK293 Cells
  • Humans
  • In Vitro Techniques
  • Lamin Type A / genetics
  • Lamin Type A / metabolism*
  • Mice
  • Muscle Fibers, Skeletal / metabolism
  • Muscular Dystrophy, Emery-Dreifuss / genetics
  • Muscular Dystrophy, Emery-Dreifuss / metabolism
  • Mutation / genetics
  • Mutation, Missense / genetics
  • Myoblasts / cytology
  • Myoblasts / metabolism
  • Protein Binding / genetics
  • Protein Binding / physiology
  • Real-Time Polymerase Chain Reaction
  • SOXB1 Transcription Factors / genetics
  • Satellite Cells, Skeletal Muscle / metabolism
  • Site-Specific DNA-Methyltransferase (Adenine-Specific) / genetics
  • Site-Specific DNA-Methyltransferase (Adenine-Specific) / metabolism

Substances

  • Lamin Type A
  • SOX2 protein, human
  • SOXB1 Transcription Factors
  • Dam methyltransferase
  • Site-Specific DNA-Methyltransferase (Adenine-Specific)