Mutations in protein N-arginine methyltransferases are not the cause of FTLD-FUS

Neurobiol Aging. 2013 Sep;34(9):2235.e11-3. doi: 10.1016/j.neurobiolaging.2013.04.004. Epub 2013 Apr 28.


The nuclear protein fused in sarcoma (FUS) is found in cytoplasmic inclusions in a subset of patients with the neurodegenerative disorder frontotemporal lobar degeneration (FTLD-FUS). FUS contains a methylated arginine-glycine-glycine domain that is required for transport into the nucleus. Recent findings have shown that this domain is hypomethylated in patients with FTLD-FUS. To determine whether the cause of hypomethylation is the result of mutations in protein N-arginine methyltransferases (PRMTs), we selected 3 candidate genes (PRMT1, PRMT3, and PRMT8) and performed complete sequencing analysis and real-time polymerase chain reaction mRNA expression analysis in 20 FTLD-FUS cases. No mutations or statistically significant changes in expression were observed in our patient samples, suggesting that defects in PRMTs are not the cause of FTLD-FUS.

Publication types

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

MeSH terms

  • 3' Untranslated Regions / genetics
  • 5' Untranslated Regions / genetics
  • DNA / genetics*
  • Frontotemporal Lobar Degeneration / genetics*
  • Humans
  • Membrane Proteins / genetics*
  • Mutation*
  • Protein-Arginine N-Methyltransferases / genetics*
  • RNA, Messenger
  • Real-Time Polymerase Chain Reaction
  • Repressor Proteins / genetics*
  • Sequence Analysis, Protein


  • 3' Untranslated Regions
  • 5' Untranslated Regions
  • Membrane Proteins
  • RNA, Messenger
  • Repressor Proteins
  • DNA
  • PRMT1 protein, human
  • PRMT3 protein, human
  • PRMT8 protein, human
  • Protein-Arginine N-Methyltransferases