메뉴 건너뛰기




Volumn 162, Issue 5, 2015, Pages 1066-1077

A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation

Author keywords

[No Author keywords available]

Indexed keywords

PRION PROTEIN; PROTEIN AGGREGATE; FUS PROTEIN, HUMAN; PRION; RNA BINDING PROTEIN;

EID: 84940403835     PISSN: 00928674     EISSN: 10974172     Source Type: Journal    
DOI: 10.1016/j.cell.2015.07.047     Document Type: Article
Times cited : (1965)

References (60)
  • 2
    • 63049091236 scopus 로고    scopus 로고
    • A systematic survey identifies prions and illuminates sequence features of prionogenic proteins
    • S. Alberti, R. Halfmann, O. King, A. Kapila, and S. Lindquist A systematic survey identifies prions and illuminates sequence features of prionogenic proteins Cell 137 2009 146 158
    • (2009) Cell , vol.137 , pp. 146-158
    • Alberti, S.1    Halfmann, R.2    King, O.3    Kapila, A.4    Lindquist, S.5
  • 3
    • 84939860220 scopus 로고    scopus 로고
    • Phase transitions of multivalent proteins can promote clustering of membrane receptors
    • S. Banjade, and M.K. Rosen Phase transitions of multivalent proteins can promote clustering of membrane receptors eLife 3 2014 3
    • (2014) ELife , vol.3 , pp. 3
    • Banjade, S.1    Rosen, M.K.2
  • 7
    • 79952723337 scopus 로고    scopus 로고
    • Active liquid-like behavior of nucleoli determines their size and shape in Xenopus laevis oocytes
    • C.P. Brangwynne, T.J. Mitchison, and A.A. Hyman Active liquid-like behavior of nucleoli determines their size and shape in Xenopus laevis oocytes Proc. Natl. Acad. Sci. USA 108 2011 4334 4339
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 4334-4339
    • Brangwynne, C.P.1    Mitchison, T.J.2    Hyman, A.A.3
  • 8
    • 35948951960 scopus 로고    scopus 로고
    • Edc3p and a glutamine/asparagine-rich domain of Lsm4p function in processing body assembly in Saccharomyces cerevisiae
    • C.J. Decker, D. Teixeira, and R. Parker Edc3p and a glutamine/asparagine-rich domain of Lsm4p function in processing body assembly in Saccharomyces cerevisiae J. Cell Biol. 179 2007 437 449
    • (2007) J. Cell Biol. , vol.179 , pp. 437-449
    • Decker, C.J.1    Teixeira, D.2    Parker, R.3
  • 9
    • 84902291718 scopus 로고    scopus 로고
    • The role of FUS gene variants in neurodegenerative diseases
    • H. Deng, K. Gao, and J. Jankovic The role of FUS gene variants in neurodegenerative diseases Nat. Rev. Neurol. 10 2014 337 348
    • (2014) Nat. Rev. Neurol. , vol.10 , pp. 337-348
    • Deng, H.1    Gao, K.2    Jankovic, J.3
  • 10
    • 38349042010 scopus 로고    scopus 로고
    • Protein phase behavior in aqueous solutions: Crystallization, liquid-liquid phase separation, gels, and aggregates
    • A.C. Dumetz, A.M. Chockla, E.W. Kaler, and A.M. Lenhoff Protein phase behavior in aqueous solutions: crystallization, liquid-liquid phase separation, gels, and aggregates Biophys. J. 94 2008 570 583
    • (2008) Biophys. J. , vol.94 , pp. 570-583
    • Dumetz, A.C.1    Chockla, A.M.2    Kaler, E.W.3    Lenhoff, A.M.4
  • 12
    • 0034612274 scopus 로고    scopus 로고
    • Control of protein crystal nucleation around the metastable liquid-liquid phase boundary
    • O. Galkin, and P.G. Vekilov Control of protein crystal nucleation around the metastable liquid-liquid phase boundary Proc. Natl. Acad. Sci. USA 97 2000 6277 6281
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6277-6281
    • Galkin, O.1    Vekilov, P.G.2
  • 14
    • 84899538596 scopus 로고    scopus 로고
    • 3D live fluorescence imaging of cellular dynamics using Bessel beam plane illumination microscopy
    • L. Gao, L. Shao, B.C. Chen, and E. Betzig 3D live fluorescence imaging of cellular dynamics using Bessel beam plane illumination microscopy Nat. Protoc. 9 2014 1083 1101
    • (2014) Nat. Protoc. , vol.9 , pp. 1083-1101
    • Gao, L.1    Shao, L.2    Chen, B.C.3    Betzig, E.4
  • 16
    • 80052802585 scopus 로고    scopus 로고
    • RNA-binding proteins with prion-like domains in ALS and FTLD-U
    • A.D. Gitler, and J. Shorter RNA-binding proteins with prion-like domains in ALS and FTLD-U Prion 5 2011 179 187
    • (2011) Prion , vol.5 , pp. 179-187
    • Gitler, A.D.1    Shorter, J.2
  • 19
    • 84886617003 scopus 로고    scopus 로고
    • Translation repressors, an RNA helicase, and developmental cues control RNP phase transitions during early development
    • A. Hubstenberger, S.L. Noble, C. Cameron, and T.C. Evans Translation repressors, an RNA helicase, and developmental cues control RNP phase transitions during early development Dev. Cell 27 2013 161 173
    • (2013) Dev. Cell , vol.27 , pp. 161-173
    • Hubstenberger, A.1    Noble, S.L.2    Cameron, C.3    Evans, T.C.4
  • 20
    • 79960285739 scopus 로고    scopus 로고
    • Beyond stereospecificity: Liquids and mesoscale organization of cytoplasm
    • A.A. Hyman, and C.P. Brangwynne Beyond stereospecificity: liquids and mesoscale organization of cytoplasm Dev. Cell 21 2011 14 16
    • (2011) Dev. Cell , vol.21 , pp. 14-16
    • Hyman, A.A.1    Brangwynne, C.P.2
  • 22
    • 84883688262 scopus 로고    scopus 로고
    • Self-propagation of pathogenic protein aggregates in neurodegenerative diseases
    • M. Jucker, and L.C. Walker Self-propagation of pathogenic protein aggregates in neurodegenerative diseases Nature 501 2013 45 51
    • (2013) Nature , vol.501 , pp. 45-51
    • Jucker, M.1    Walker, L.C.2
  • 23
    • 84860872161 scopus 로고    scopus 로고
    • Cell-free formation of RNA granules: Low complexity sequence domains form dynamic fibers within hydrogels
    • M. Kato, T.W. Han, S. Xie, K. Shi, X. Du, L.C. Wu, H. Mirzaei, E.J. Goldsmith, J. Longgood, J. Pei, and et al. Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels Cell 149 2012 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
  • 26
    • 84862151933 scopus 로고    scopus 로고
    • The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease
    • O.D. King, A.D. Gitler, and J. Shorter The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease Brain Res. 1462 2012 61 80
    • (2012) Brain Res. , vol.1462 , pp. 61-80
    • King, O.D.1    Gitler, A.D.2    Shorter, J.3
  • 30
  • 32
    • 84878661360 scopus 로고    scopus 로고
    • Stress granules as crucibles of ALS pathogenesis
    • Y.R. Li, O.D. King, J. Shorter, and A.D. Gitler Stress granules as crucibles of ALS pathogenesis J. Cell Biol. 201 2013 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
  • 33
  • 34
    • 80053555789 scopus 로고    scopus 로고
    • More than just a focus: The chromatin response to DNA damage and its role in genome integrity maintenance
    • J. Lukas, C. Lukas, and J. Bartek More than just a focus: The chromatin response to DNA damage and its role in genome integrity maintenance Nat. Cell Biol. 13 2011 1161 1169
    • (2011) Nat. Cell Biol. , vol.13 , pp. 1161-1169
    • Lukas, J.1    Lukas, C.2    Bartek, J.3
  • 35
    • 84876288161 scopus 로고    scopus 로고
    • Protein disorder, prion propensities, and self-organizing macromolecular collectives
    • L. Malinovska, S. Kroschwald, and S. Alberti Protein disorder, prion propensities, and self-organizing macromolecular collectives Biochim. Biophys. Acta 1834 2013 918 931
    • (2013) Biochim. Biophys. Acta , vol.1834 , pp. 918-931
    • Malinovska, L.1    Kroschwald, S.2    Alberti, S.3
  • 36
    • 84883136968 scopus 로고    scopus 로고
    • The RNA-binding protein fused in sarcoma (FUS) functions downstream of poly(ADP-ribose) polymerase (PARP) in response to DNA damage
    • A.S. Mastrocola, S.H. Kim, A.T. Trinh, L.A. Rodenkirch, and R.S. Tibbetts The RNA-binding protein fused in sarcoma (FUS) functions downstream of poly(ADP-ribose) polymerase (PARP) in response to DNA damage J. Biol. Chem. 288 2013 24731 24741
    • (2013) J. Biol. Chem. , vol.288 , pp. 24731-24741
    • Mastrocola, A.S.1    Kim, S.H.2    Trinh, A.T.3    Rodenkirch, L.A.4    Tibbetts, R.S.5
  • 37
    • 77957364208 scopus 로고    scopus 로고
    • Anisotropies in cortical tension reveal the physical basis of polarizing cortical flows
    • M. Mayer, M. Depken, J.S. Bois, F. Jülicher, and S.W. Grill Anisotropies in cortical tension reveal the physical basis of polarizing cortical flows Nature 467 2010 617 621
    • (2010) Nature , vol.467 , pp. 617-621
    • Mayer, M.1    Depken, M.2    Bois, J.S.3    Jülicher, F.4    Grill, S.W.5
  • 38
    • 84891947306 scopus 로고    scopus 로고
    • Intranuclear aggregation of mutant FUS/TLS as a molecular pathomechanism of amyotrophic lateral sclerosis
    • T. Nomura, S. Watanabe, K. Kaneko, K. Yamanaka, N. Nukina, and Y. Furukawa Intranuclear aggregation of mutant FUS/TLS as a molecular pathomechanism of amyotrophic lateral sclerosis J. Biol. Chem. 289 2014 1192 1202
    • (2014) J. Biol. Chem. , vol.289 , pp. 1192-1202
    • Nomura, T.1    Watanabe, S.2    Kaneko, K.3    Yamanaka, K.4    Nukina, N.5    Furukawa, Y.6
  • 42
    • 84882801549 scopus 로고    scopus 로고
    • Altered ribostasis: RNA-protein granules in degenerative disorders
    • M. Ramaswami, J.P. Taylor, and R. Parker Altered ribostasis: RNA-protein granules in degenerative disorders Cell 154 2013 727 736
    • (2013) Cell , vol.154 , pp. 727-736
    • Ramaswami, M.1    Taylor, J.P.2    Parker, R.3
  • 46
    • 84907489769 scopus 로고    scopus 로고
    • Multistep process of FUS aggregation in the cell cytoplasm involves RNA-dependent and RNA-independent mechanisms
    • T.A. Shelkovnikova, H.K. Robinson, J.A. Southcombe, N. Ninkina, and V.L. Buchman Multistep process of FUS aggregation in the cell cytoplasm involves RNA-dependent and RNA-independent mechanisms Hum. Mol. Genet. 23 2014 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
  • 48
    • 79955502687 scopus 로고    scopus 로고
    • Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLS
    • Z. Sun, Z. Diaz, X. Fang, M.P. Hart, A. Chesi, J. Shorter, and A.D. Gitler Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLS PLoS Biol. 9 2011 e1000614
    • (2011) PLoS Biol. , vol.9 , pp. e1000614
    • Sun, Z.1    Diaz, Z.2    Fang, X.3    Hart, M.P.4    Chesi, A.5    Shorter, J.6    Gitler, A.D.7
  • 50
    • 84906877425 scopus 로고    scopus 로고
    • Assemblages: Functional units formed by cellular phase separation
    • J.A. Toretsky, and P.E. Wright Assemblages: functional units formed by cellular phase separation J. Cell Biol. 206 2014 579 588
    • (2014) J. Cell Biol. , vol.206 , pp. 579-588
    • Toretsky, J.A.1    Wright, P.E.2
  • 52
    • 4143146536 scopus 로고    scopus 로고
    • Dense liquid precursor for the nucleation of ordered solid phases from solution
    • P.G. Vekilov Dense liquid precursor for the nucleation of ordered solid phases from solution Cryst. Growth Des. 4 2004 671 685
    • (2004) Cryst. Growth Des. , vol.4 , pp. 671-685
    • Vekilov, P.G.1
  • 53
    • 77958095167 scopus 로고    scopus 로고
    • Phase transitions of folded proteins
    • P.G. Vekilov Phase transitions of folded proteins Soft Matter 6 2010 5254 5272
    • (2010) Soft Matter , vol.6 , pp. 5254-5272
    • Vekilov, P.G.1
  • 56
    • 84861964894 scopus 로고    scopus 로고
    • Getting RNA and protein in phase
    • S.C. Weber, and C.P. Brangwynne Getting RNA and protein in phase Cell 149 2012 1188 1191
    • (2012) Cell , vol.149 , pp. 1188-1191
    • Weber, S.C.1    Brangwynne, C.P.2
  • 57
    • 84874040052 scopus 로고    scopus 로고
    • Dual specificity kinase DYRK3 couples stress granule condensation/dissolution to mTORC1 signaling
    • F. Wippich, B. Bodenmiller, M.G. Trajkovska, S. Wanka, R. Aebersold, and L. Pelkmans Dual specificity kinase DYRK3 couples stress granule condensation/dissolution to mTORC1 signaling Cell 152 2013 791 805
    • (2013) Cell , vol.152 , pp. 791-805
    • Wippich, F.1    Bodenmiller, B.2    Trajkovska, M.G.3    Wanka, S.4    Aebersold, R.5    Pelkmans, L.6
  • 58
    • 84910081742 scopus 로고    scopus 로고
    • A "proteomic ruler" for protein copy number and concentration estimation without spike-in standards
    • J.R. Wis̈niewski, M.Y. Hein, J. Cox, and M. Mann A "proteomic ruler" for protein copy number and concentration estimation without spike-in standards Mol. Cell. Proteomics 13 2014 3497 3506
    • (2014) Mol. Cell. Proteomics , vol.13 , pp. 3497-3506
    • Wis̈niewski, J.R.1    Hein, M.Y.2    Cox, J.3    Mann, M.4
  • 59
    • 77950788517 scopus 로고    scopus 로고
    • FUS-immunoreactive intranuclear inclusions in neurodegenerative disease
    • J. Woulfe, D.A. Gray, and I.R. Mackenzie FUS-immunoreactive intranuclear inclusions in neurodegenerative disease Brain Pathol. 20 2010 589 597
    • (2010) Brain Pathol. , vol.20 , pp. 589-597
    • Woulfe, J.1    Gray, D.A.2    Mackenzie, I.R.3
  • 60
    • 84919338450 scopus 로고    scopus 로고
    • Self-assembled FUS binds active chromatin and regulates gene transcription
    • L. Yang, J. Gal, J. Chen, and H. Zhu Self-assembled FUS binds active chromatin and regulates gene transcription Proc. Natl. Acad. Sci. USA 111 2014 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.