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Volumn 24, Issue 18, 2015, Pages 5174-5183

Subcellular localization and RNAs determine FUS architecture in different cellular compartments

Author keywords

[No Author keywords available]

Indexed keywords

CYTOPLASM PROTEIN; FUSED IN SARCOMA PROTEIN; MUTANT PROTEIN; NUCLEAR PROTEIN; NUCLEAR RNA; CHROMATIN; RNA; RNA BINDING PROTEIN FUS;

EID: 84940659038     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddv239     Document Type: Article
Times cited : (24)

References (39)
  • 3
    • 0035978743 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis
    • Rowland, L.P. and Shneider, N.A. (2001) Amyotrophic lateral sclerosis. N. Engl. J. Med., 344, 1688-1700.
    • (2001) N. Engl. J. Med , vol.344 , pp. 1688-1700
    • Rowland, L.P.1    Shneider, N.A.2
  • 5
    • 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 e2327-2340.
    • (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
  • 6
    • 39949085583 scopus 로고    scopus 로고
    • Stress granules: the Tao of RNA triage
    • Anderson, P. and Kedersha, N. (2008) Stress granules: the Tao of RNA triage. Trends Biochem. Sci., 33, 141-150.
    • (2008) Trends Biochem. Sci , vol.33 , pp. 141-150
    • Anderson, P.1    Kedersha, N.2
  • 7
    • 84881220788 scopus 로고    scopus 로고
    • FUS/TLS assembles into stress granules and is a prosurvival factor during hyperosmolar stress
    • Sama, R.R., Ward, C.L., Kaushansky, L.J., Lemay, N., Ishigaki, S., Urano, F. and Bosco, D.A. (2013) FUS/TLS assembles into stress granules and is a prosurvival factor during hyperosmolar stress. J. Cell. Physiol., 228, 2222-2231.
    • (2013) J. Cell. Physiol , vol.228 , pp. 2222-2231
    • Sama, R.R.1    Ward, C.L.2    Kaushansky, L.J.3    Lemay, N.4    Ishigaki, S.5    Urano, F.6    Bosco, D.A.7
  • 8
    • 48249083430 scopus 로고    scopus 로고
    • The multifunctional FUS, EWS and TAF15 proto-oncoproteins show cell type-specific expression patterns and involvement in cell spreading and stress response
    • Andersson, M.K., Stahlberg, A., Arvidsson, Y., Olofsson, A., Semb, H., Stenman, G., Nilsson, O. and Aman, P. (2008) The multifunctional FUS, EWS and TAF15 proto-oncoproteins show cell type-specific expression patterns and involvement in cell spreading and stress response. BMC Cell Biol., 9, 37.
    • (2008) BMC Cell Biol , vol.9 , pp. 37
    • Andersson, M.K.1    Stahlberg, A.2    Arvidsson, Y.3    Olofsson, A.4    Semb, H.5    Stenman, G.6    Nilsson, O.7    Aman, P.8
  • 10
    • 84907533335 scopus 로고    scopus 로고
    • Aggregation of ALSlinked FUS mutant sequesters RNA binding proteins and impairs RNA granules formation
    • Takanashi, K. and Yamaguchi, A. (2014) Aggregation of ALSlinked FUS mutant sequesters RNA binding proteins and impairs RNA granules formation. Biochem. Biophys. Res. Commun., 452, 600-607.
    • (2014) Biochem. Biophys. Res. Commun , vol.452 , pp. 600-607
    • Takanashi, K.1    Yamaguchi, A.2
  • 11
    • 84911386329 scopus 로고    scopus 로고
    • Autophagy regulates amyotrophic lateral sclerosis-linked fused in sarcoma-positive stress granules in neurons
    • Ryu, H.H., Jun, M.H., Min, K.J., Jang, D.J., Lee, Y.S., Kim, H.K. and Lee, J.A. (2014) Autophagy regulates amyotrophic lateral sclerosis-linked fused in sarcoma-positive stress granules in neurons. Neurobiol. Aging, 35, 2822-2831.
    • (2014) Neurobiol. Aging , vol.35 , pp. 2822-2831
    • Ryu, H.H.1    Jun, M.H.2    Min, K.J.3    Jang, D.J.4    Lee, Y.S.5    Kim, H.K.6    Lee, J.A.7
  • 12
    • 84878661360 scopus 로고    scopus 로고
    • Stress granules as crucibles of ALS pathogenesis
    • Li, Y.R., King, O.D., Shorter, J. and Gitler, A.D. (2013) Stress granules as crucibles of ALS pathogenesis. J. Cell Biol., 201, 361-372.
    • (2013) J. Cell Biol , vol.201 , pp. 361-372
    • Li, Y.R.1    King, O.D.2    Shorter, J.3    Gitler, A.D.4
  • 13
    • 84878873344 scopus 로고    scopus 로고
    • Inclusions in frontotemporal lobar degeneration with TDP-43 proteinopathy (FTLD-TDP) and amyotrophic lateral sclerosis (ALS), but not FTLD with FUS proteinopathy (FTLDFUS), have properties of amyloid
    • Bigio, E.H., Wu, J.Y., Deng, H.X., Bit-Ivan, E.N., Mao, Q., Ganti, R., Peterson, M., Siddique, N., Geula, C., Siddique, T. et al. (2013) Inclusions in frontotemporal lobar degeneration with TDP-43 proteinopathy (FTLD-TDP) and amyotrophic lateral sclerosis (ALS), but not FTLD with FUS proteinopathy (FTLDFUS), have properties of amyloid. Acta Neuropathol., 125, 463-465.
    • (2013) Acta Neuropathol , vol.125 , pp. 463-465
    • Bigio, E.H.1    Wu, J.Y.2    Deng, H.X.3    Bit-Ivan, E.N.4    Mao, Q.5    Ganti, R.6    Peterson, M.7    Siddique, N.8    Geula, C.9    Siddique, T.10
  • 14
    • 84907489769 scopus 로고    scopus 로고
    • Multistep process of FUS aggregation in the cell cytoplasm involves RNA-dependent and RNA-independent mechanisms
    • Shelkovnikova, T.A., Robinson, H.K., Southcombe, J.A., Ninkina, N. and Buchman, V.L. (2014) Multistep process of FUS aggregation in the cell cytoplasm involves RNA-dependent and RNA-independent mechanisms. Hum. Mol. Genet., 23, 5211-5226.
    • (2014) Hum. Mol. Genet , vol.23 , pp. 5211-5226
    • Shelkovnikova, T.A.1    Robinson, H.K.2    Southcombe, J.A.3    Ninkina, N.4    Buchman, V.L.5
  • 15
    • 84919338450 scopus 로고    scopus 로고
    • Self-assembled FUS binds active chromatin and regulates gene transcription
    • Yang, L., Gal, J., Chen, J. and Zhu, H. (2014) Self-assembled FUS binds active chromatin and regulates gene transcription. Proc. Natl Acad. Sci. USA, 111, 17809-17814.
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 17809-17814
    • Yang, L.1    Gal, J.2    Chen, J.3    Zhu, H.4
  • 17
    • 84877342846 scopus 로고    scopus 로고
    • Genome wide array analysis indicates that an amyotrophic lateral sclerosis mutation of FUS causes an early increase of CAMK2N2 in vitro
    • Convertini, P., Zhang, J., de la Grange, P., Hayward, L.J., Zhu, H. and Stamm, S. (2013) Genome wide array analysis indicates that an amyotrophic lateral sclerosis mutation of FUS causes an early increase of CAMK2N2 in vitro. Biochim. Biophys. Acta, 1832, 1129-1135.
    • (2013) Biochim. Biophys. Acta , vol.1832 , pp. 1129-1135
    • Convertini, P.1    Zhang, J.2    de la Grange, P.3    Hayward, L.J.4    Zhu, H.5    Stamm, S.6
  • 18
    • 84862151933 scopus 로고    scopus 로고
    • The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease
    • King, O.D., Gitler, A.D. and Shorter, J. (2012) The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease. Brain Res., 1462, 61-80.
    • (2012) Brain Res , vol.1462 , pp. 61-80
    • King, O.D.1    Gitler, A.D.2    Shorter, J.3
  • 19
    • 79955502687 scopus 로고    scopus 로고
    • Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLS
    • Sun, Z., Diaz, Z., Fang, X., Hart, M.P., Chesi, A., Shorter, J. and Gitler, A.D. (2011) Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLS. PLoS Biol., 9, e1000614.
    • (2011) PLoS Biol , vol.9
    • Sun, Z.1    Diaz, Z.2    Fang, X.3    Hart, M.P.4    Chesi, A.5    Shorter, J.6    Gitler, A.D.7
  • 22
    • 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
  • 23
    • 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
  • 25
    • 77956384199 scopus 로고    scopus 로고
    • Novel missense and truncating mutations in FUS/TLS in familial ALS
    • Waibel, S., Neumann, M., Rabe, M., Meyer, T. and Ludolph, A.C. (2010) Novel missense and truncating mutations in FUS/TLS in familial ALS. Neurology, 75, 815-817.
    • (2010) Neurology , vol.75 , pp. 815-817
    • Waibel, S.1    Neumann, M.2    Rabe, M.3    Meyer, T.4    Ludolph, A.C.5
  • 29
    • 84871807395 scopus 로고    scopus 로고
    • The RRM domain of human fused in sarcoma protein reveals a non-canonical nucleic acid binding site
    • Liu, X., Niu, C., Ren, J., Zhang, J., Xie, X., Zhu, H., Feng, W. and Gong, W. (2013) The RRM domain of human fused in sarcoma protein reveals a non-canonical nucleic acid binding site. Biochim. Biophys. Acta, 1832, 375-385.
    • (2013) Biochim. Biophys. Acta , vol.1832 , pp. 375-385
    • Liu, X.1    Niu, C.2    Ren, J.3    Zhang, J.4    Xie, X.5    Zhu, H.6    Feng, W.7    Gong, W.8
  • 30
    • 84860872161 scopus 로고    scopus 로고
    • Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels
    • Kato, M., Han, T.W., Xie, S., Shi, K., Du, X., Wu, L.C., Mirzaei, H., Goldsmith, E.J., Longgood, J., Pei, J. et al. (2012) Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels. Cell, 149, 753-767.
    • (2012) Cell , vol.149 , pp. 753-767
    • Kato, M.1    Han, T.W.2    Xie, S.3    Shi, K.4    Du, X.5    Wu, L.C.6    Mirzaei, H.7    Goldsmith, E.J.8    Longgood, J.9    Pei, J.10
  • 31
    • 33644899679 scopus 로고    scopus 로고
    • Intracellular conformational alterations of mutant SOD1 and the implications for fALS-associated SOD1 mutant induced motor neuron cell death
    • Zhang, F. and Zhu, H. (2006) Intracellular conformational alterations of mutant SOD1 and the implications for fALS-associated SOD1 mutant induced motor neuron cell death. Biochim. Biophys. Acta, 1760, 404-414.
    • (2006) Biochim. Biophys. Acta , vol.1760 , pp. 404-414
    • Zhang, F.1    Zhu, H.2
  • 32
    • 53049090386 scopus 로고    scopus 로고
    • Interaction of amyotrophic lateral sclerosis (ALS)-related mutant copper-zinc superoxide dismutase with the dynein-dynactin complex contributes to inclusion formation
    • Strom, A.L., Shi, P., Zhang, F., Gal, J., Kilty, R., Hayward, L.J. and Zhu, H. (2008) Interaction of amyotrophic lateral sclerosis (ALS)-related mutant copper-zinc superoxide dismutase with the dynein-dynactin complex contributes to inclusion formation. J. Biol. Chem., 283, 22795-22805.
    • (2008) J. Biol. Chem , vol.283 , pp. 22795-22805
    • Strom, A.L.1    Shi, P.2    Zhang, F.3    Gal, J.4    Kilty, R.5    Hayward, L.J.6    Zhu, H.7
  • 33
    • 0031932169 scopus 로고    scopus 로고
    • Protein aggregation: folding aggregates, inclusion bodies and amyloid
    • Fink, A.L. (1998) Protein aggregation: folding aggregates, inclusion bodies and amyloid. Fold. Des., 3, R9-R23.
    • (1998) Fold. Des , vol.3 , pp. R9-R23
    • Fink, A.L.1
  • 39
    • 84858726202 scopus 로고    scopus 로고
    • Motor neuron apoptosis and neuromuscular junction perturbation are prominent features in a Drosophila model of Fusmediated ALS
    • Xia, R., Liu, Y., Yang, L., Gal, J., Zhu, H. and Jia, J. (2012) Motor neuron apoptosis and neuromuscular junction perturbation are prominent features in a Drosophila model of Fusmediated ALS. Mol. Neurodegener., 7, 10.
    • (2012) Mol. Neurodegener , vol.7 , pp. 10
    • Xia, R.1    Liu, Y.2    Yang, L.3    Gal, J.4    Zhu, H.5    Jia, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.