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Volumn 128, Issue 22, 2015, Pages 4151-4159

Phosphorylation of C-terminal tyrosine residue 526 in FUS impairs its nuclear import

Author keywords

Amyotrophic lateral sclerosis; Frontotemporal lobar degeneration; FUS; Nuclear import; Phosphorylation; Transportin 1

Indexed keywords

TYROSINE; FUS PROTEIN, HUMAN; KARYOPHERIN BETA; RNA BINDING PROTEIN FUS; TNPO1 PROTEIN, HUMAN;

EID: 84949844936     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.176602     Document Type: Article
Times cited : (25)

References (54)
  • 2
    • 77955897545 scopus 로고    scopus 로고
    • Juvenile ALS with basophilic inclusions is a FUS proteinopathy with FUS mutations
    • Baumer, D., Hilton, D., Paine, S. M. L., Turner, M. R., Lowe, J., Talbot, K. and Ansorge, O. (2010). Juvenile ALS with basophilic inclusions is a FUS proteinopathy with FUS mutations. Neurology 75, 611-618.
    • (2010) Neurology , vol.75 , pp. 611-618
    • Baumer, D.1    Hilton, D.2    Paine, S.M.L.3    Turner, M.R.4    Lowe, J.5    Talbot, K.6    Ansorge, O.7
  • 3
    • 17444381645 scopus 로고    scopus 로고
    • Delocalization of the multifunctional RNA splicing factor TLS/FUS in hippocampal neurones: exclusion from the nucleus and accumulation in dendritic granules and spine heads
    • Belly, A., Moreau-Gachelin, F., Sadoul, R. and Goldberg, Y. (2005). Delocalization of the multifunctional RNA splicing factor TLS/FUS in hippocampal neurones: exclusion from the nucleus and accumulation in dendritic granules and spine heads. Neurosci. Lett. 379, 152-157.
    • (2005) Neurosci. Lett. , vol.379 , pp. 152-157
    • Belly, A.1    Moreau-Gachelin, F.2    Sadoul, R.3    Goldberg, Y.4
  • 5
    • 2942564430 scopus 로고    scopus 로고
    • Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence
    • Blom, N., Sicheritz-Pontén, T., Gupta, R., Gammeltoft, S. and Brunak, S. (2004). Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence. Proteomics 4, 1633-1649.
    • (2004) Proteomics , vol.4 , pp. 1633-1649
    • Blom, N.1    Sicheritz-Pontén, T.2    Gupta, R.3    Gammeltoft, S.4    Brunak, S.5
  • 10
    • 22244475384 scopus 로고    scopus 로고
    • Tyrosine 394 is phosphorylated in Alzheimer's paired helical filament tau and in fetal tau with c-Abl as the candidate tyrosine kinase
    • Derkinderen, P., Scales, T. M. E., Hanger, D. P., Leung, K.-Y., Byers, H. L., Ward, M. A., Lenz, C., Price, C., Bird, I. N., Perera, T. et al. (2005). Tyrosine 394 is phosphorylated in Alzheimer's paired helical filament tau and in fetal tau with c-Abl as the candidate tyrosine kinase. J. Neurosci. 25, 6584-6593.
    • (2005) J. Neurosci. , vol.25 , pp. 6584-6593
    • Derkinderen, P.1    Scales, T.M.E.2    Hanger, D.P.3    Leung, K.-Y.4    Byers, H.L.5    Ward, M.A.6    Lenz, C.7    Price, C.8    Bird, I.N.9    Perera, T.10
  • 14
    • 80053646130 scopus 로고    scopus 로고
    • Nuclear localization sequence of FUS and induction of stress granules by ALS mutants
    • Gal, J., Zhang, J., Kwinter, D. M., Zhai, J., Jia, H., Jia, J. and Zhu, H. (2011). Nuclear localization sequence of FUS and induction of stress granules by ALS mutants. Neurobiol. Aging 32, 2323.e2327-e2340.
    • (2011) Neurobiol. Aging , vol.32 , pp. 2323.e2327-e2340
    • Gal, J.1    Zhang, J.2    Kwinter, D.M.3    Zhai, J.4    Jia, H.5    Jia, J.6    Zhu, H.7
  • 15
    • 0025953405 scopus 로고
    • Use of vanadate as protein-phosphotyrosine phosphatase inhibitor
    • Gordon, J. A. (1991). Use of vanadate as protein-phosphotyrosine phosphatase inhibitor. Methods Enzymol. 201, 477-482.
    • (1991) Methods Enzymol. , vol.201 , pp. 477-482
    • Gordon, J.A.1
  • 18
    • 68949200962 scopus 로고    scopus 로고
    • Proteomic analysis of methylarginine-containing proteins in HeLa cells by two-dimensional gel electrophoresis and immunoblotting with a methylarginine-specific antibody
    • Hung, C.-J., Lee, Y.-J., Chen, D.-H. and Li, C. (2009). Proteomic analysis of methylarginine-containing proteins in HeLa cells by two-dimensional gel electrophoresis and immunoblotting with a methylarginine-specific antibody. Protein J. 28, 139-147.
    • (2009) Protein J. , vol.28 , pp. 139-147
    • Hung, C.-J.1    Lee, Y.-J.2    Chen, D.-H.3    Li, C.4
  • 23
    • 33746776838 scopus 로고    scopus 로고
    • Rules for nuclear localization sequence recognition by karyopherin beta 2
    • Lee, B. J., Cansizoglu, A. E., Süel, K. E., Louis, T. H., Zhang, Z. and Chook, Y. M. (2006). Rules for nuclear localization sequence recognition by karyopherin beta 2. Cell 126, 543-558.
    • (2006) Cell , vol.126 , pp. 543-558
    • Lee, B.J.1    Cansizoglu, A.E.2    Süel, K.E.3    Louis, T.H.4    Zhang, Z.5    Chook, Y.M.6
  • 24
    • 79959354904 scopus 로고    scopus 로고
    • Tyrosine Phosphorylation in the C-Terminal nuclear localization and retention signal (C-NLS) of the EWS protein
    • Leemann-Zakaryan, R. P., Pahlich, S., Grossenbacher, D. and Gehring, H. (2011). Tyrosine Phosphorylation in the C-Terminal nuclear localization and retention signal (C-NLS) of the EWS protein. Sarcoma 2011, 218483.
    • (2011) Sarcoma , vol.2011 , pp. 218483
    • Leemann-Zakaryan, R.P.1    Pahlich, S.2    Grossenbacher, D.3    Gehring, H.4
  • 27
    • 79959615773 scopus 로고    scopus 로고
    • Pathological heterogeneity in amyotrophic lateral sclerosis with FUS mutations: two distinct patterns correlating with disease severity and mutation
    • Mackenzie, I. R. A., Ansorge, O., Strong, M., Bilbao, J., Zinman, L., Ang, L.-C., Baker, M., Stewart, H., Eisen, A., Rademakers, R. et al. (2011). Pathological heterogeneity in amyotrophic lateral sclerosis with FUS mutations: two distinct patterns correlating with disease severity and mutation. Acta Neuropathol. 122, 87-98.
    • (2011) Acta Neuropathol. , vol.122 , pp. 87-98
    • Mackenzie, I.R.A.1    Ansorge, O.2    Strong, M.3    Bilbao, J.4    Zinman, L.5    Ang, L.-C.6    Baker, M.7    Stewart, H.8    Eisen, A.9    Rademakers, R.10
  • 28
    • 84864547364 scopus 로고    scopus 로고
    • Domains involved in TAF15 subcellular localisation: dependence on cell type and ongoing transcription
    • Marko, M., Vlassis, A., Guialis, A. and Leichter, M. (2012). Domains involved in TAF15 subcellular localisation: dependence on cell type and ongoing transcription. Gene 506, 331-338.
    • (2012) Gene , vol.506 , pp. 331-338
    • Marko, M.1    Vlassis, A.2    Guialis, A.3    Leichter, M.4
  • 29
    • 34250209501 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis
    • Mitchell, J. D. and Borasio, G. D. (2007). Amyotrophic lateral sclerosis. Lancet 369, 2031-2041.
    • (2007) Lancet , vol.369 , pp. 2031-2041
    • Mitchell, J.D.1    Borasio, G.D.2
  • 33
    • 80052959701 scopus 로고    scopus 로고
    • FET proteins TAF15 and EWS are selective markers that distinguish FTLD with FUS pathology from amyotrophic lateral sclerosis with FUS mutations
    • Neumann, M., Bentmann, E., Dormann, D., Jawaid, A., DeJesus-Hernandez, M., Ansorge, O., Roeber, S., Kretzschmar, H. A., Munoz, D. G., Kusaka, H. et al. (2011). FET proteins TAF15 and EWS are selective markers that distinguish FTLD with FUS pathology from amyotrophic lateral sclerosis with FUS mutations. Brain 134, 2595-2609.
    • (2011) Brain , vol.134 , pp. 2595-2609
    • Neumann, M.1    Bentmann, E.2    Dormann, D.3    Jawaid, A.4    DeJesus-Hernandez, M.5    Ansorge, O.6    Roeber, S.7    Kretzschmar, H.A.8    Munoz, D.G.9    Kusaka, H.10
  • 34
    • 84871019907 scopus 로고    scopus 로고
    • Transportin 1 accumulates specifically with FET proteins but no other transportin cargos in FTLD-FUS and is absent in FUS inclusions in ALS with FUS mutations
    • Neumann, M., Valori, C. F., Ansorge, O., Kretzschmar, H. A., Munoz, D. G., Kusaka, H., Yokota, O., Ishihara, K., Ang, L.-C., Bilbao, J. M. et al. (2012). Transportin 1 accumulates specifically with FET proteins but no other transportin cargos in FTLD-FUS and is absent in FUS inclusions in ALS with FUS mutations. Acta Neuropathol. 124, 705-716.
    • (2012) Acta Neuropathol. , vol.124 , pp. 705-716
    • Neumann, M.1    Valori, C.F.2    Ansorge, O.3    Kretzschmar, H.A.4    Munoz, D.G.5    Kusaka, H.6    Yokota, O.7    Ishihara, K.8    Ang, L.-C.9    Bilbao, J.M.10
  • 35
    • 77953019135 scopus 로고    scopus 로고
    • Nuclear import impairment causes cytoplasmic trans-activation response DNA-binding protein accumulation and is associated with frontotemporal lobar degeneration
    • Nishimura, A. L., Zupunski, V., Troakes, C., Kathe, C., Fratta, P., Howell, M., Gallo, J.-M., Hortobagyi, T., Shaw, C. E. and Rogelj, B. (2010). Nuclear import impairment causes cytoplasmic trans-activation response DNA-binding protein accumulation and is associated with frontotemporal lobar degeneration. Brain 133, 1763-1771.
    • (2010) Brain , vol.133 , pp. 1763-1771
    • Nishimura, A.L.1    Zupunski, V.2    Troakes, C.3    Kathe, C.4    Fratta, P.5    Howell, M.6    Gallo, J.-M.7    Hortobagyi, T.8    Shaw, C.E.9    Rogelj, B.10
  • 36
    • 84867290759 scopus 로고    scopus 로고
    • FUS-NLS/Transportin 1 complex structure provides insights into the nuclear targeting mechanism of FUS and the implications in ALS
    • Niu, C., Zhang, J., Gao, F., Yang, L., Jia, M., Zhu, H. and Gong, W. (2012). FUS-NLS/Transportin 1 complex structure provides insights into the nuclear targeting mechanism of FUS and the implications in ALS. PLoS ONE 7, e47056.
    • (2012) PLoS ONE , vol.7
    • Niu, C.1    Zhang, J.2    Gao, F.3    Yang, L.4    Jia, M.5    Zhu, H.6    Gong, W.7
  • 38
    • 0038000050 scopus 로고    scopus 로고
    • Detection of arginine dimethylated peptides by parallel precursor ion scanning mass spectrometry in positive ion mode
    • Rappsilber, J., Friesen, W. J., Paushkin, S., Dreyfuss, G. and Mann, M. (2003). Detection of arginine dimethylated peptides by parallel precursor ion scanning mass spectrometry in positive ion mode. Anal Chem. 75, 3107-3114.
    • (2003) Anal Chem. , vol.75 , pp. 3107-3114
    • Rappsilber, J.1    Friesen, W.J.2    Paushkin, S.3    Dreyfuss, G.4    Mann, M.5
  • 42
    • 79959605078 scopus 로고    scopus 로고
    • The most common type of FTLD-FUS (aFTLD-U) is associated with a distinct clinical form of frontotemporal dementia but is not related to mutations in the FUS gene
    • Snowden, J. S., Hu, Q., Rollinson, S., Halliwell, N., Robinson, A., Davidson, Y. S., Momeni, P., Baborie, A., Griffiths, T. D., Jaros, E. et al. (2011). The most common type of FTLD-FUS (aFTLD-U) is associated with a distinct clinical form of frontotemporal dementia but is not related to mutations in the FUS gene. Acta Neuropathol. 122, 99-110.
    • (2011) Acta Neuropathol. , vol.122 , pp. 99-110
    • Snowden, J.S.1    Hu, Q.2    Rollinson, S.3    Halliwell, N.4    Robinson, A.5    Davidson, Y.S.6    Momeni, P.7    Baborie, A.8    Griffiths, T.D.9    Jaros, E.10
  • 43
    • 36749081534 scopus 로고    scopus 로고
    • Crossing the nuclear envelope: hierarchical regulation of nucleocytoplasmic transport
    • Terry, L. J., Shows, E. B. and Wente, S. R. (2007). Crossing the nuclear envelope: hierarchical regulation of nucleocytoplasmic transport. Science 318, 1412-1416.
    • (2007) Science , vol.318 , pp. 1412-1416
    • Terry, L.J.1    Shows, E.B.2    Wente, S.R.3
  • 44
    • 83455162720 scopus 로고    scopus 로고
    • Arginine methylation by PRMT1 regulates nuclear-cytoplasmic localization and toxicity of FUS/TLS harbouring ALS-linked mutations
    • Tradewell, M. L., Yu, Z., Tibshirani, M., Boulanger, M.-C., Durham, H. D. and Richard, S. (2012). Arginine methylation by PRMT1 regulates nuclear-cytoplasmic localization and toxicity of FUS/TLS harbouring ALS-linked mutations. Hum. Mol. Genet. 21, 136-149.
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 136-149
    • Tradewell, M.L.1    Yu, Z.2    Tibshirani, M.3    Boulanger, M.-C.4    Durham, H.D.5    Richard, S.6
  • 45
    • 84880177442 scopus 로고    scopus 로고
    • Transportin 1 colocalization with Fused in Sarcoma (FUS) inclusions is not characteristic for amyotrophic lateral sclerosis-FUS confirming disrupted nuclear import of mutant FUS and distinguishing it fromfrontotemporal lobar degeneration with FUS inclusions
    • Troakes, C., Hortobágyi, T., Vance, C., Al-Sarraj, S., Rogelj, B. and Shaw, C. E. (2013). Transportin 1 colocalization with Fused in Sarcoma (FUS) inclusions is not characteristic for amyotrophic lateral sclerosis-FUS confirming disrupted nuclear import of mutant FUS and distinguishing it fromfrontotemporal lobar degeneration with FUS inclusions. Neuropathol. Appl. Neurobiol. 39, 553-561.
    • (2013) Neuropathol. Appl. Neurobiol. , vol.39 , pp. 553-561
    • Troakes, C.1    Hortobágyi, T.2    Vance, C.3    Al-Sarraj, S.4    Rogelj, B.5    Shaw, C.E.6
  • 48
    • 79961025441 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of tau regulates its interactions with Fyn SH2 domains, but not SH3 domains, altering the cellular localization of tau
    • Usardi, A., Pooler, A. M., Seereeram, A., Reynolds, C. H., Derkinderen, P., Anderton, B., Hanger, D. P., Noble, W. and Williamson, R. (2011). Tyrosine phosphorylation of tau regulates its interactions with Fyn SH2 domains, but not SH3 domains, altering the cellular localization of tau. FEBS J. 278, 2927-2937.
    • (2011) FEBS J. , vol.278 , pp. 2927-2937
    • Usardi, A.1    Pooler, A.M.2    Seereeram, A.3    Reynolds, C.H.4    Derkinderen, P.5    Anderton, B.6    Hanger, D.P.7    Noble, W.8    Williamson, R.9
  • 49
    • 84866490231 scopus 로고    scopus 로고
    • The molecular basis of the frontotemporal lobar degeneration-amyotrophic lateral sclerosis spectrum
    • Van Langenhove, T., van der Zee, J. and Van Broeckhoven, C. (2012). The molecular basis of the frontotemporal lobar degeneration-amyotrophic lateral sclerosis spectrum. Ann. Med. 44, 817-828.
    • (2012) Ann. Med. , vol.44 , pp. 817-828
    • Van Langenhove, T.1    van der Zee, J.2    Van Broeckhoven, C.3
  • 52
    • 84869005887 scopus 로고    scopus 로고
    • The effect of PRMT1-mediated arginine methylation on the subcellular localization, stress granules, and detergent-insoluble aggregates of FUS/TLS
    • Yamaguchi, A. and Kitajo, K. (2012). The effect of PRMT1-mediated arginine methylation on the subcellular localization, stress granules, and detergent-insoluble aggregates of FUS/TLS. PLoS ONE 7, e49267.
    • (2012) PLoS ONE , vol.7
    • Yamaguchi, A.1    Kitajo, K.2
  • 53
    • 33748786259 scopus 로고    scopus 로고
    • Identification and characterization of the nuclear localization/retention signal in the EWS proto-oncoprotein
    • Zakaryan, R. P. and Gehring, H. (2006). Identification and characterization of the nuclear localization/retention signal in the EWS proto-oncoprotein. J. Mol. Biol. 363, 27-38.
    • (2006) J. Mol. Biol. , vol.363 , pp. 27-38
    • Zakaryan, R.P.1    Gehring, H.2
  • 54
    • 84864366184 scopus 로고    scopus 로고
    • Structural and energetic basis of ALS-causing mutations in the atypical proline-tyrosine nuclear localization signal of the Fused in Sarcoma protein (FUS)
    • Zhang, Z. C. and Chook, Y. M. (2012). Structural and energetic basis of ALS-causing mutations in the atypical proline-tyrosine nuclear localization signal of the Fused in Sarcoma protein (FUS). Proc. Natl. Acad. Sci. USA 109, 12017-12021.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 12017-12021
    • Zhang, Z.C.1    Chook, Y.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.