메뉴 건너뛰기




Volumn 164, Issue 3, 2016, Pages 487-498

ATPase-Modulated Stress Granules Contain a Diverse Proteome and Substructure

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; PROTEOME; AATF PROTEIN, HUMAN; APOPTOSIS REGULATORY PROTEIN; DEAD BOX PROTEIN; DED1 PROTEIN, S CEREVISIAE; MESSENGER RNA; REPRESSOR PROTEIN; RIBONUCLEOPROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN; SODIUM AZIDE;

EID: 84955625345     PISSN: 00928674     EISSN: 10974172     Source Type: Journal    
DOI: 10.1016/j.cell.2015.12.038     Document Type: Article
Times cited : (1087)

References (54)
  • 1
    • 59349118696 scopus 로고    scopus 로고
    • A genetically encoded fluorescent reporter of ATP:ADP ratio
    • J. Berg, Y.P. Hung, and G. Yellen A genetically encoded fluorescent reporter of ATP:ADP ratio Nat. Methods 6 2009 161 166
    • (2009) Nat. Methods , vol.6 , pp. 161-166
    • Berg, J.1    Hung, Y.P.2    Yellen, G.3
  • 4
    • 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
  • 5
    • 34347387606 scopus 로고    scopus 로고
    • Accumulation of polyadenylated mRNA, Pab1p, eIF4E, and eIF4G with P-bodies in Saccharomyces cerevisiae
    • M. Brengues, and R. Parker Accumulation of polyadenylated mRNA, Pab1p, eIF4E, and eIF4G with P-bodies in Saccharomyces cerevisiae Mol. Biol. Cell 18 2007 2592 2602
    • (2007) Mol. Biol. Cell , vol.18 , pp. 2592-2602
    • Brengues, M.1    Parker, R.2
  • 6
    • 84920847059 scopus 로고    scopus 로고
    • MRNP granules. Assembly, function, and connections with disease
    • J.R. Buchan mRNP granules. Assembly, function, and connections with disease RNA Biol. 11 2014 1019 1030
    • (2014) RNA Biol. , vol.11 , pp. 1019-1030
    • Buchan, J.R.1
  • 7
    • 72149095755 scopus 로고    scopus 로고
    • Eukaryotic stress granules: The ins and outs of translation
    • J.R. Buchan, and R. Parker Eukaryotic stress granules: the ins and outs of translation Mol. Cell 36 2009 932 941
    • (2009) Mol. Cell , vol.36 , pp. 932-941
    • Buchan, J.R.1    Parker, R.2
  • 8
    • 56149086182 scopus 로고    scopus 로고
    • P bodies promote stress granule assembly in Saccharomyces cerevisiae
    • J.R. Buchan, D. Muhlrad, and R. Parker P bodies promote stress granule assembly in Saccharomyces cerevisiae J. Cell Biol. 183 2008 441 455
    • (2008) J. Cell Biol. , vol.183 , pp. 441-455
    • Buchan, J.R.1    Muhlrad, D.2    Parker, R.3
  • 9
    • 79251554956 scopus 로고    scopus 로고
    • Stress-specific composition, assembly and kinetics of stress granules in Saccharomyces cerevisiae
    • J.R. Buchan, J.-H. Yoon, and R. Parker Stress-specific composition, assembly and kinetics of stress granules in Saccharomyces cerevisiae J. Cell Sci. 124 2011 228 239
    • (2011) J. Cell Sci. , vol.124 , pp. 228-239
    • Buchan, J.R.1    Yoon, J.-H.2    Parker, R.3
  • 10
    • 84879349589 scopus 로고    scopus 로고
    • Eukaryotic stress granules are cleared by autophagy and Cdc48/VCP function
    • J.R. Buchan, R.-M. Kolaitis, J.P. Taylor, and R. Parker Eukaryotic stress granules are cleared by autophagy and Cdc48/VCP function Cell 153 2013 1461 1474
    • (2013) Cell , vol.153 , pp. 1461-1474
    • Buchan, J.R.1    Kolaitis, R.-M.2    Taylor, J.P.3    Parker, R.4
  • 12
    • 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
  • 13
    • 84858374665 scopus 로고    scopus 로고
    • The amyloid state of proteins in human diseases
    • D. Eisenberg, and M. Jucker The amyloid state of proteins in human diseases Cell 148 2012 1188 1203
    • (2012) Cell , vol.148 , pp. 1188-1203
    • Eisenberg, D.1    Jucker, M.2
  • 16
    • 0042349629 scopus 로고    scopus 로고
    • Yeast aspartyl-tRNA synthetase binds specifically its own mRNA
    • M. Frugier, and R. Giegé Yeast aspartyl-tRNA synthetase binds specifically its own mRNA J. Mol. Biol. 331 2003 375 383
    • (2003) J. Mol. Biol. , vol.331 , pp. 375-383
    • Frugier, M.1    Giegé, R.2
  • 18
    • 79960040173 scopus 로고    scopus 로고
    • An ALS-associated mutation affecting TDP-43 enhances protein aggregation, fibril formation and neurotoxicity
    • W. Guo, Y. Chen, X. Zhou, A. Kar, P. Ray, X. Chen, E.J. Rao, M. Yang, H. Ye, L. Zhu, and et al. An ALS-associated mutation affecting TDP-43 enhances protein aggregation, fibril formation and neurotoxicity Nat. Struct. Mol. Biol. 18 2011 822 830
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 822-830
    • Guo, W.1    Chen, Y.2    Zhou, X.3    Kar, A.4    Ray, P.5    Chen, X.6    Rao, E.J.7    Yang, M.8    Ye, H.9    Zhu, L.10
  • 19
    • 80053022305 scopus 로고    scopus 로고
    • The DEAD-box protein Ded1 modulates translation by the formation and resolution of an eIF4F-mRNA complex
    • A. Hilliker, Z. Gao, E. Jankowsky, and R. Parker The DEAD-box protein Ded1 modulates translation by the formation and resolution of an eIF4F-mRNA complex Mol. Cell 43 2011 962 972
    • (2011) Mol. Cell , vol.43 , pp. 962-972
    • Hilliker, A.1    Gao, Z.2    Jankowsky, E.3    Parker, R.4
  • 20
    • 84876591791 scopus 로고    scopus 로고
    • Vanillin inhibits translation and induces messenger ribonucleoprotein (mRNP) granule formation in saccharomyces cerevisiae: Application and validation of high-content, image-based profiling
    • A. Iwaki, S. Ohnuki, Y. Suga, S. Izawa, and Y. Ohya Vanillin inhibits translation and induces messenger ribonucleoprotein (mRNP) granule formation in saccharomyces cerevisiae: application and validation of high-content, image-based profiling PLoS ONE 8 2013 e61748
    • (2013) PLoS ONE , vol.8 , pp. e61748
    • Iwaki, A.1    Ohnuki, S.2    Suga, Y.3    Izawa, S.4    Ohya, Y.5
  • 22
    • 84855199318 scopus 로고    scopus 로고
    • The R2TP complex: Discovery and functions
    • Y. Kakihara, and W.A. Houry The R2TP complex: discovery and functions Biochim. Biophys. Acta 1823 2012 101 107
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 101-107
    • Kakihara, Y.1    Houry, W.A.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
    • 84940503517 scopus 로고    scopus 로고
    • Promiscuous interactions and protein disaggregases determine the material state of stress-inducible RNP granules
    • S. Kroschwald, S. Maharana, D. Mateju, L. Malinovska, E. Nüske, I. Poser, D. Richter, and S. Alberti Promiscuous interactions and protein disaggregases determine the material state of stress-inducible RNP granules eLife 4 2015 e06807
    • (2015) ELife , vol.4 , pp. e06807
    • Kroschwald, S.1    Maharana, S.2    Mateju, D.3    Malinovska, L.4    Nüske, E.5    Poser, I.6    Richter, D.7    Alberti, S.8
  • 27
    • 0034595448 scopus 로고    scopus 로고
    • Uninterrupted MCM2-7 function required for DNA replication fork progression
    • K. Labib, J.A. Tercero, and J.F. Diffley Uninterrupted MCM2-7 function required for DNA replication fork progression Science 288 2000 1643 1647
    • (2000) Science , vol.288 , pp. 1643-1647
    • Labib, K.1    Tercero, J.A.2    Diffley, J.F.3
  • 29
    • 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
  • 30
    • 84944884978 scopus 로고    scopus 로고
    • Formation and Maturation of Phase-Separated Liquid Droplets by RNA-Binding Proteins
    • Y. Lin, D.S.W. Protter, M.K. Rosen, and R. Parker Formation and Maturation of Phase-Separated Liquid Droplets by RNA-Binding Proteins Mol. Cell 60 2015 208 219
    • (2015) Mol. Cell , vol.60 , pp. 208-219
    • Lin, Y.1    Protter, D.S.W.2    Rosen, M.K.3    Parker, R.4
  • 31
    • 70450285065 scopus 로고    scopus 로고
    • Dynein and kinesin regulate stress-granule and P-body dynamics
    • M. Loschi, C.C. Leishman, N. Berardone, and G.L. Boccaccio Dynein and kinesin regulate stress-granule and P-body dynamics J. Cell Sci. 122 2009 3973 3982
    • (2009) J. Cell Sci. , vol.122 , pp. 3973-3982
    • Loschi, M.1    Leishman, C.C.2    Berardone, N.3    Boccaccio, G.L.4
  • 33
    • 84944907005 scopus 로고    scopus 로고
    • Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization
    • A. Molliex, J. Temirov, J. Lee, M. Coughlin, A.P. Kanagaraj, H.J. Kim, T. Mittag, and J.P. Taylor Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization Cell 163 2015 123 133
    • (2015) Cell , vol.163 , pp. 123-133
    • Molliex, A.1    Temirov, J.2    Lee, J.3    Coughlin, M.4    Kanagaraj, A.P.5    Kim, H.J.6    Mittag, T.7    Taylor, J.P.8
  • 36
    • 53349165578 scopus 로고    scopus 로고
    • A functional RNAi screen links O-GlcNAc modification of ribosomal proteins to stress granule and processing body assembly
    • T. Ohn, N. Kedersha, T. Hickman, S. Tisdale, and P. Anderson A functional RNAi screen links O-GlcNAc modification of ribosomal proteins to stress granule and processing body assembly Nat. Cell Biol. 10 2008 1224 1231
    • (2008) Nat. Cell Biol. , vol.10 , pp. 1224-1231
    • Ohn, T.1    Kedersha, N.2    Hickman, T.3    Tisdale, S.4    Anderson, P.5
  • 37
    • 33947727395 scopus 로고    scopus 로고
    • Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex
    • S.S. Patel, B.J. Belmont, J.M. Sante, and M.F. Rexach Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex Cell 129 2007 83 96
    • (2007) Cell , vol.129 , pp. 83-96
    • Patel, S.S.1    Belmont, B.J.2    Sante, J.M.3    Rexach, M.F.4
  • 38
    • 40349089746 scopus 로고    scopus 로고
    • High-efficiency rotating point spread functions
    • S.R.P. Pavani, and R. Piestun High-efficiency rotating point spread functions Opt. Express 16 2008 3484 3489
    • (2008) Opt. Express , vol.16 , pp. 3484-3489
    • Pavani, S.R.P.1    Piestun, R.2
  • 40
    • 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
  • 41
    • 50249131374 scopus 로고    scopus 로고
    • A role for Q/N-rich aggregation-prone regions in P-body localization
    • M.A.M. Reijns, R.D. Alexander, M.P. Spiller, and J.D. Beggs A role for Q/N-rich aggregation-prone regions in P-body localization J. Cell Sci. 121 2008 2463 2472
    • (2008) J. Cell Sci. , vol.121 , pp. 2463-2472
    • Reijns, M.A.M.1    Alexander, R.D.2    Spiller, M.P.3    Beggs, J.D.4
  • 42
    • 0037013954 scopus 로고    scopus 로고
    • The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion
    • K. Ribbeck, and D. Görlich The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion EMBO J. 21 2002 2664 2671
    • (2002) EMBO J. , vol.21 , pp. 2664-2671
    • Ribbeck, K.1    Görlich, D.2
  • 43
    • 84907222725 scopus 로고    scopus 로고
    • RNA Function. RNA and dynamic nuclear organization
    • J. Rinn, and M. Guttman RNA Function. RNA and dynamic nuclear organization Science 345 2014 1240 1241
    • (2014) Science , vol.345 , pp. 1240-1241
    • Rinn, J.1    Guttman, M.2
  • 45
    • 0034601464 scopus 로고    scopus 로고
    • A chromatin remodelling complex involved in transcription and DNA processing
    • X. Shen, G. Mizuguchi, A. Hamiche, and C. Wu A chromatin remodelling complex involved in transcription and DNA processing Nature 406 2000 541 544
    • (2000) Nature , vol.406 , pp. 541-544
    • Shen, X.1    Mizuguchi, G.2    Hamiche, A.3    Wu, C.4
  • 46
    • 33748752207 scopus 로고    scopus 로고
    • The replicative helicases of bacteria, archaea, and eukarya can unwind RNA-DNA hybrid substrates
    • J.-H. Shin, and Z. Kelman The replicative helicases of bacteria, archaea, and eukarya can unwind RNA-DNA hybrid substrates J. Biol. Chem. 281 2006 26914 26921
    • (2006) J. Biol. Chem. , vol.281 , pp. 26914-26921
    • Shin, J.-H.1    Kelman, Z.2
  • 48
    • 33749177252 scopus 로고    scopus 로고
    • The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions
    • S. Tam, R. Geller, C. Spiess, and J. Frydman The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions Nat. Cell Biol. 8 2006 1155 1162
    • (2006) Nat. Cell Biol. , vol.8 , pp. 1155-1162
    • Tam, S.1    Geller, R.2    Spiess, C.3    Frydman, J.4
  • 49
    • 84938923219 scopus 로고    scopus 로고
    • Drosophila germ granules are structured and contain homotypic mRNA clusters
    • T. Trcek, M. Grosch, A. York, H. Shroff, T. Lionnet, and R. Lehmann Drosophila germ granules are structured and contain homotypic mRNA clusters Nat. Commun. 6 2015 7962
    • (2015) Nat. Commun. , vol.6 , pp. 7962
    • Trcek, T.1    Grosch, M.2    York, A.3    Shroff, H.4    Lionnet, T.5    Lehmann, R.6
  • 50
  • 51
    • 84939780690 scopus 로고    scopus 로고
    • Differential effects of Ydj1 and Sis1 on Hsp70-mediated clearance of stress granules in Saccharomyces cerevisiae
    • R.W. Walters, D. Muhlrad, J. Garcia, and R. Parker Differential effects of Ydj1 and Sis1 on Hsp70-mediated clearance of stress granules in Saccharomyces cerevisiae RNA 21 2015 1660 1671
    • (2015) RNA , vol.21 , pp. 1660-1671
    • Walters, R.W.1    Muhlrad, D.2    Garcia, J.3    Parker, R.4
  • 52
    • 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
  • 54
    • 77953157170 scopus 로고    scopus 로고
    • Dcp2 phosphorylation by Ste20 modulates stress granule assembly and mRNA decay in Saccharomyces cerevisiae
    • J.-H. Yoon, E.-J. Choi, and R. Parker Dcp2 phosphorylation by Ste20 modulates stress granule assembly and mRNA decay in Saccharomyces cerevisiae J. Cell Biol. 189 2010 813 827
    • (2010) J. Cell Biol. , vol.189 , pp. 813-827
    • Yoon, J.-H.1    Choi, E.-J.2    Parker, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.