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 Anthony Josephs, Bradley F Boeve, Ronald Carl Petersen, Glenda M. Halliday, Jillian Kril, John C. van Swieten, William W. Seeley, Dennis W Dickson, Rosa V Rademakers

Research output: Contribution to journalArticle

6 Citations (Scopus)

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)
JournalNeurobiology of Aging
Volume34
Issue number9
DOIs
StatePublished - Sep 2013

Fingerprint

Protein-Arginine N-Methyltransferases
Frontotemporal Lobar Degeneration
Sarcoma
Mutation
Glycine
Inclusion Bodies
Nuclear Proteins
Neurodegenerative Diseases
Arginine
Real-Time Polymerase Chain Reaction
Messenger RNA

Keywords

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

ASJC Scopus subject areas

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

Cite this

Mutations in protein N-arginine methyltransferases are not the cause of FTLD-FUS. / Ravenscroft, Thomas A.; Baker, Matt C.; Rutherford, Nicola J.; Neumann, Manuela; Mackenzie, Ian R.; Josephs, Keith Anthony; Boeve, Bradley F; Petersen, Ronald Carl; Halliday, Glenda M.; Kril, Jillian; van Swieten, John C.; Seeley, William W.; Dickson, Dennis W; Rademakers, Rosa V.

In: Neurobiology of Aging, Vol. 34, No. 9, 09.2013.

Research output: Contribution to journalArticle

Ravenscroft, TA, Baker, MC, Rutherford, NJ, Neumann, M, Mackenzie, IR, Josephs, KA, Boeve, BF, Petersen, RC, Halliday, GM, Kril, J, van Swieten, JC, Seeley, WW, Dickson, DW & Rademakers, RV 2013, 'Mutations in protein N-arginine methyltransferases are not the cause of FTLD-FUS', Neurobiology of Aging, vol. 34, no. 9. https://doi.org/10.1016/j.neurobiolaging.2013.04.004
Ravenscroft, Thomas A. ; Baker, Matt C. ; Rutherford, Nicola J. ; Neumann, Manuela ; Mackenzie, Ian R. ; Josephs, Keith Anthony ; Boeve, Bradley F ; Petersen, Ronald Carl ; Halliday, Glenda M. ; Kril, Jillian ; van Swieten, John C. ; Seeley, William W. ; Dickson, Dennis W ; Rademakers, Rosa V. / Mutations in protein N-arginine methyltransferases are not the cause of FTLD-FUS. In: Neurobiology of Aging. 2013 ; Vol. 34, No. 9.
@article{b25bc271808e4b3c82a874ffa0be3216,
title = "Mutations in protein N-arginine methyltransferases are not the cause of FTLD-FUS",
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.",
keywords = "FET proteins, Frontotemporal lobar degeneration, FUS, PRMT1, PRMT3, PRMT8, Protein N-arginine methyltransferase",
author = "Ravenscroft, {Thomas A.} and Baker, {Matt C.} and Rutherford, {Nicola J.} and Manuela Neumann and Mackenzie, {Ian R.} and Josephs, {Keith Anthony} and Boeve, {Bradley F} and Petersen, {Ronald Carl} and Halliday, {Glenda M.} and Jillian Kril and {van Swieten}, {John C.} and Seeley, {William W.} and Dickson, {Dennis W} and Rademakers, {Rosa V}",
year = "2013",
month = "9",
doi = "10.1016/j.neurobiolaging.2013.04.004",
language = "English (US)",
volume = "34",
journal = "Neurobiology of Aging",
issn = "0197-4580",
publisher = "Elsevier Inc.",
number = "9",

}

TY - JOUR

T1 - Mutations in protein N-arginine methyltransferases are not the cause of FTLD-FUS

AU - Ravenscroft, Thomas A.

AU - Baker, Matt C.

AU - Rutherford, Nicola J.

AU - Neumann, Manuela

AU - Mackenzie, Ian R.

AU - Josephs, Keith Anthony

AU - Boeve, Bradley F

AU - Petersen, Ronald Carl

AU - Halliday, Glenda M.

AU - Kril, Jillian

AU - van Swieten, John C.

AU - Seeley, William W.

AU - Dickson, Dennis W

AU - Rademakers, Rosa V

PY - 2013/9

Y1 - 2013/9

N2 - 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.

AB - 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.

KW - FET proteins

KW - Frontotemporal lobar degeneration

KW - FUS

KW - PRMT1

KW - PRMT3

KW - PRMT8

KW - Protein N-arginine methyltransferase

UR - http://www.scopus.com/inward/record.url?scp=84878943012&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84878943012&partnerID=8YFLogxK

U2 - 10.1016/j.neurobiolaging.2013.04.004

DO - 10.1016/j.neurobiolaging.2013.04.004

M3 - Article

C2 - 23635657

AN - SCOPUS:84878943012

VL - 34

JO - Neurobiology of Aging

JF - Neurobiology of Aging

SN - 0197-4580

IS - 9

ER -