Home > Publications Database > Arginine methylation next to the PY-NLS modulates Transportin binding and nuclear import of FUS. > print

001     136697
005     20240619104245.0
024 7 _ |a 10.1038/emboj.2012.261
|2 doi
024 7 _ |a pmid:22968170
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024 7 _ |a pmc:PMC3501225
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024 7 _ |a 0261-4189
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024 7 _ |a 1460-2075
|2 ISSN
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037 _ _ |a DZNE-2020-03019
041 _ _ |a English
082 _ _ |a 570
100 1 _ |a Dormann, Dorothee
|0 P:(DE-2719)9000059
|b 0
|e First author
245 _ _ |a Arginine methylation next to the PY-NLS modulates Transportin binding and nuclear import of FUS.
260 _ _ |a Hoboken, NJ [u.a.]
|c 2012
|b Wiley
264 _ 1 |3 online
|2 Crossref
|b Wiley
|c 2012-09-11
264 _ 1 |3 print
|2 Crossref
|b Wiley
|c 2012-11-14
336 7 _ |a article
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336 7 _ |a Output Types/Journal article
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336 7 _ |a Journal Article
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336 7 _ |a ARTICLE
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336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a Journal Article
|0 0
|2 EndNote
520 _ _ |a Fused in sarcoma (FUS) is a nuclear protein that carries a proline-tyrosine nuclear localization signal (PY-NLS) and is imported into the nucleus via Transportin (TRN). Defects in nuclear import of FUS have been implicated in neurodegeneration, since mutations in the PY-NLS of FUS cause amyotrophic lateral sclerosis (ALS). Moreover, FUS is deposited in the cytosol in a subset of frontotemporal lobar degeneration (FTLD) patients. Here, we show that arginine methylation modulates nuclear import of FUS via a novel TRN-binding epitope. Chemical or genetic inhibition of arginine methylation restores TRN-mediated nuclear import of ALS-associated FUS mutants. The unmethylated arginine-glycine-glycine domain preceding the PY-NLS interacts with TRN and arginine methylation in this domain reduces TRN binding. Inclusions in ALS-FUS patients contain methylated FUS, while inclusions in FTLD-FUS patients are not methylated. Together with recent findings that FUS co-aggregates with two related proteins of the FET family and TRN in FTLD-FUS but not in ALS-FUS, our study provides evidence that these two diseases may be initiated by distinct pathomechanisms and implicates alterations in arginine methylation in pathogenesis.
536 _ _ |a 344 - Clinical and Health Care Research (POF3-344)
|0 G:(DE-HGF)POF3-344
|c POF3-344
|f POF III
|x 0
542 _ _ |i 2015-09-01
|2 Crossref
|u http://doi.wiley.com/10.1002/tdm_license_1.1
588 _ _ |a Dataset connected to CrossRef, PubMed,
650 _ 7 |a Karyopherins
|2 NLM Chemicals
650 _ 7 |a Nuclear Localization Signals
|2 NLM Chemicals
650 _ 7 |a RNA-Binding Protein FUS
|2 NLM Chemicals
650 _ 7 |a Repressor Proteins
|2 NLM Chemicals
650 _ 7 |a Tyrosine
|0 42HK56048U
|2 NLM Chemicals
650 _ 7 |a Arginine
|0 94ZLA3W45F
|2 NLM Chemicals
650 _ 7 |a Proline
|0 9DLQ4CIU6V
|2 NLM Chemicals
650 _ 7 |a PRMT1 protein, human
|0 EC 2.1.1.319
|2 NLM Chemicals
650 _ 7 |a Protein-Arginine N-Methyltransferases
|0 EC 2.1.1.319
|2 NLM Chemicals
650 _ 2 |a Active Transport, Cell Nucleus
|2 MeSH
650 _ 2 |a Amino Acid Sequence
|2 MeSH
650 _ 2 |a Amyotrophic Lateral Sclerosis: genetics
|2 MeSH
650 _ 2 |a Amyotrophic Lateral Sclerosis: metabolism
|2 MeSH
650 _ 2 |a Arginine: metabolism
|2 MeSH
650 _ 2 |a Cell Nucleus: metabolism
|2 MeSH
650 _ 2 |a Frontotemporal Lobar Degeneration: metabolism
|2 MeSH
650 _ 2 |a Gene Silencing
|2 MeSH
650 _ 2 |a HeLa Cells
|2 MeSH
650 _ 2 |a Humans
|2 MeSH
650 _ 2 |a Karyopherins: genetics
|2 MeSH
650 _ 2 |a Karyopherins: metabolism
|2 MeSH
650 _ 2 |a Methylation
|2 MeSH
650 _ 2 |a Molecular Sequence Data
|2 MeSH
650 _ 2 |a Nuclear Localization Signals: metabolism
|2 MeSH
650 _ 2 |a Proline: metabolism
|2 MeSH
650 _ 2 |a Protein Binding
|2 MeSH
650 _ 2 |a Protein-Arginine N-Methyltransferases: genetics
|2 MeSH
650 _ 2 |a Protein-Arginine N-Methyltransferases: metabolism
|2 MeSH
650 _ 2 |a RNA-Binding Protein FUS: genetics
|2 MeSH
650 _ 2 |a RNA-Binding Protein FUS: metabolism
|2 MeSH
650 _ 2 |a Repressor Proteins: genetics
|2 MeSH
650 _ 2 |a Repressor Proteins: metabolism
|2 MeSH
650 _ 2 |a Signal Transduction
|2 MeSH
650 _ 2 |a Tyrosine: metabolism
|2 MeSH
700 1 _ |a Madl, Tobias
|0 P:(DE-HGF)0
|b 1
700 1 _ |a Valori, Chiara F
|0 P:(DE-2719)2810632
|b 2
700 1 _ |a Bentmann, Eva
|0 P:(DE-HGF)0
|b 3
700 1 _ |a Tahirovic, Sabina
|0 P:(DE-HGF)0
|b 4
700 1 _ |a Abou-Ajram, Claudia
|0 P:(DE-HGF)0
|b 5
700 1 _ |a Kremmer, Elisabeth
|0 P:(DE-HGF)0
|b 6
700 1 _ |a Ansorge, Olaf
|0 P:(DE-HGF)0
|b 7
700 1 _ |a Mackenzie, Ian R A
|0 P:(DE-HGF)0
|b 8
700 1 _ |a Neumann, Manuela
|0 P:(DE-2719)2810592
|b 9
700 1 _ |a Haass, Christian
|0 P:(DE-HGF)0
|b 10
773 1 8 |a 10.1038/emboj.2012.261
|b : Wiley, 2012-09-11
|n 22
|p 4258-4275
|3 journal-article
|2 Crossref
|t The EMBO Journal
|v 31
|y 2012
|x 0261-4189
773 _ _ |a 10.1038/emboj.2012.261
|g Vol. 31, no. 22, p. 4258 - 4275
|0 PERI:(DE-600)1467419-1
|n 22
|q 31:22<4258 - 4275
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|t The EMBO journal
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856 7 _ |2 Pubmed Central
|u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3501225
856 4 _ |u https://pub.dzne.de/record/136697/files/DZNE-2020-03019_Restricted.pdf
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