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

Thomas A. Ravenscroft, Matt C. Baker, Nicola J. Rutherford, Manuela Neumann, Ian R. Mackenzie, Keith A. Josephs, Bradley F. Boeve, Ronald Petersen, Glenda M. Halliday, Jillian Kril, John C. van Swieten, William W. Seeley, Dennis W. Dickson, Rosa Rademakers

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)2235.e11-2235.e13
JournalNeurobiology of aging
Volume34
Issue number9
DOIs
StatePublished - Sep 2013

Keywords

  • FET proteins
  • FUS
  • Frontotemporal lobar degeneration
  • PRMT1
  • PRMT3
  • PRMT8
  • Protein N-arginine methyltransferase

ASJC Scopus subject areas

  • Neuroscience(all)
  • Aging
  • Clinical Neurology
  • Developmental Biology
  • Geriatrics and Gerontology

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