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Volumn 5, Issue Se, 2016, Pages

Distinct stages in stress granule assembly and disassembly

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; INITIATION FACTOR 2ALPHA; STRESS GRANULE; UNCLASSIFIED DRUG; 1,6 HEXANEDIOL; ARSENITE SODIUM; ARSENOUS ACID DERIVATIVE; CYCLOHEXIMIDE; DIGITONIN; GLYCOL; INTRINSICALLY DISORDERED PROTEIN; MESSENGER RIBONUCLEOPROTEIN; MESSENGER RNA; RIBONUCLEOPROTEIN; SODIUM DERIVATIVE;

EID: 84986185216     PISSN: None     EISSN: 2050084X     Source Type: Journal    
DOI: 10.7554/eLife.18413     Document Type: Article
Times cited : (566)

References (49)
  • 1
    • 84893364894 scopus 로고    scopus 로고
    • Phase transitions and size scaling of membrane-less organelles
    • Brangwynne CP. 2013. Phase transitions and size scaling of membrane-less organelles. The Journal of Cell Biology 203:875–881. doi: 10.1083/jcb.201308087
    • (2013) The Journal of Cell Biology , vol.203 , pp. 875-881
    • Brangwynne, C.P.1
  • 3
    • 84946554664 scopus 로고    scopus 로고
    • Polymer physics of intracellular phase transitions
    • Brangwynne CP, Tompa P, Pappu RV. 2015. Polymer physics of intracellular phase transitions. Nature Physics 11: 899–904. doi: 10.1038/nphys3532
    • (2015) Nature Physics , vol.11 , pp. 899-904
    • Brangwynne, C.P.1    Tompa, P.2    Pappu, R.V.3
  • 4
    • 84879349589 scopus 로고    scopus 로고
    • Eukaryotic stress granules are cleared by autophagy and Cdc48/VCP function
    • Buchan JR, Kolaitis RM, Taylor JP, Parker R. 2013. Eukaryotic stress granules are cleared by autophagy and Cdc48/VCP function. Cell 153:1461–1474. doi: 10.1016/j.cell.2013.05.037
    • (2013) Cell , vol.153 , pp. 1461-1474
    • Buchan, J.R.1    Kolaitis, R.M.2    Taylor, J.P.3    Parker, R.4
  • 5
    • 72149095755 scopus 로고    scopus 로고
    • Eukaryotic stress granules: The ins and outs of translation
    • Buchan JR, Parker R. 2009. Eukaryotic stress granules: the ins and outs of translation. Molecular Cell 36:932–941. doi: 10.1016/j.molcel.2009.11.020
    • (2009) Molecular Cell , vol.36 , pp. 932-941
    • Buchan, J.R.1    Parker, R.2
  • 6
    • 84920847059 scopus 로고    scopus 로고
    • MRNP granules. Assembly, function, and connections with disease
    • Buchan JR. 2014. mRNP granules. Assembly, function, and connections with disease. RNA Biology 11:1019–1030. doi: 10.4161/15476286.2014.972208
    • (2014) RNA Biology , vol.11 , pp. 1019-1030
    • Buchan, J.R.1
  • 7
    • 73649097951 scopus 로고    scopus 로고
    • Role of microtubules in stress granule assembly: Microtubule dynamical instability favors the formation of micrometric stress granules in cells
    • Chernov KG, Barbet A, Hamon L, Ovchinnikov LP, Curmi PA, Pastré D. 2009. Role of microtubules in stress granule assembly: microtubule dynamical instability favors the formation of micrometric stress granules in cells. The Journal of Biological Chemistry 284:36569–36580. doi: 10.1074/jbc.M109.042879
    • (2009) The Journal of Biological Chemistry , vol.284 , pp. 36569-36580
    • Chernov, K.G.1    Barbet, A.2    Hamon, L.3    Ovchinnikov, L.P.4    Curmi, P.A.5    Pastré, D.6
  • 8
    • 35948951960 scopus 로고    scopus 로고
    • Edc3p and a glutamine/asparagine-rich domain of Lsm4p function in processing body assembly in Saccharomyces cerevisiae
    • Decker CJ, Teixeira D, Parker R. 2007. Edc3p and a glutamine/asparagine-rich domain of Lsm4p function in processing body assembly in Saccharomyces cerevisiae. The Journal of Cell Biology 179:437–449. doi: 10.1083/jcb.200704147
    • (2007) The Journal of Cell Biology , vol.179 , pp. 437-449
    • Decker, C.J.1    Teixeira, D.2    Parker, R.3
  • 10
    • 84930960021 scopus 로고    scopus 로고
    • The disordered P granule protein LAF-1 drives phase separation into droplets with tunable viscosity and dynamics
    • Elbaum-Garfinkle S, Kim Y, Szczepaniak K, Chen CC-H, Eckmann CR, Myong S, Brangwynne CP. 2015. The disordered P granule protein LAF-1 drives phase separation into droplets with tunable viscosity and dynamics. PNAS 112:7189–7194. doi: 10.1073/pnas.1504822112
    • (2015) PNAS , vol.112 , pp. 7189-7194
    • Elbaum-Garfinkle, S.1    Kim, Y.2    Szczepaniak, K.3    Chen, C.-H.4    Eckmann, C.R.5    Myong, S.6    Brangwynne, C.P.7
  • 12
    • 34547679515 scopus 로고    scopus 로고
    • A saturated FG-repeat hydrogel can reproduce the permeability properties of nuclear pore complexes
    • Frey S, Görlich D. 2007. A saturated FG-repeat hydrogel can reproduce the permeability properties of nuclear pore complexes. Cell 130:512–523. doi: 10.1016/j.cell.2007.06.024
    • (2007) Cell , vol.130 , pp. 512-523
    • Frey, S.1    Görlich, D.2
  • 15
    • 84860863700 scopus 로고    scopus 로고
    • Cell-free formation of RNA granules: Bound RNAs identify features and components of cellular assemblies
    • Han TW, Kato M, Xie S, Wu LC, Mirzaei H, Pei J, Chen M, Xie Y, Allen J, Xiao G, McKnight SL. 2012. Cell-free formation of RNA granules: bound RNAs identify features and components of cellular assemblies. Cell 149: 768–779. doi: 10.1016/j.cell.2012.04.016
    • (2012) Cell , vol.149 , pp. 768-779
    • Han, T.W.1    Kato, M.2    Xie, S.3    Wu, L.C.4    Mirzaei, H.5    Pei, J.6    Chen, M.7    Xie, Y.8    Allen, J.9    Xiao, G.10    McKnight, S.L.11
  • 16
    • 84865560483 scopus 로고    scopus 로고
    • Cell biology. Beyond oil and water–phase transitions in cells
    • Hyman AA, Simons K. 2012. Cell biology. Beyond oil and water–phase transitions in cells. Science 337:1047–1049. doi: 10.1126/science.1223728
    • (2012) Science , vol.337 , pp. 1047-1049
    • Hyman, A.A.1    Simons, K.2
  • 18
    • 84865260520 scopus 로고    scopus 로고
    • The permeability of reconstituted nuclear pores provides direct evidence for the selective phase model
    • Hülsmann BB, Labokha AA, Görlich D. 2012. The permeability of reconstituted nuclear pores provides direct evidence for the selective phase model. Cell 150:738–751. doi: 10.1016/j.cell.2012.07.019
    • (2012) Cell , vol.150 , pp. 738-751
    • Hülsmann, B.B.1    Labokha, A.A.2    Görlich, D.3
  • 19
    • 0142026265 scopus 로고    scopus 로고
    • Disruption of microtubules inhibits cytoplasmic ribonucleoprotein stress granule formation
    • Ivanov PA, Chudinova EM, Nadezhdina ES. 2003. Disruption of microtubules inhibits cytoplasmic ribonucleoprotein stress granule formation. Experimental Cell Research 290:227–233. doi: 10.1016/S0014-4827(03)00290-8
    • (2003) Experimental Cell Research , vol.290 , pp. 227-233
    • Ivanov, P.A.1    Chudinova, E.M.2    Nadezhdina, E.S.3
  • 21
    • 84955625345 scopus 로고    scopus 로고
    • ATPase-Modulated Stress Granules Contain a Diverse Proteome and Substructure
    • Jain S, Wheeler JR, Walters RW, Agrawal A, Barsic A, Parker R. 2016. ATPase-Modulated Stress Granules Contain a Diverse Proteome and Substructure. Cell 164:487–498. doi: 10.1016/j.cell.2015.12.038
    • (2016) Cell , vol.164 , pp. 487-498
    • Jain, S.1    Wheeler, J.R.2    Walters, R.W.3    Agrawal, A.4    Barsic, A.5    Parker, R.6
  • 23
    • 84884587610 scopus 로고    scopus 로고
    • Stress granules and cell signaling: More than just a passing phase?
    • Kedersha N, Ivanov P, Anderson P. 2013. Stress granules and cell signaling: more than just a passing phase? Trends in Biochemical Sciences 38:494–506. doi: 10.1016/j.tibs.2013.07.004
    • (2013) Trends in Biochemical Sciences , vol.38 , pp. 494-506
    • Kedersha, N.1    Ivanov, P.2    Erson, P.3
  • 24
    • 57749192735 scopus 로고    scopus 로고
    • Real-time and quantitative imaging of mammalian stress granules and processing bodies
    • Kedersha N, Tisdale S, Hickman T, Anderson P. 2008. Real-time and quantitative imaging of mammalian stress granules and processing bodies. Methods in Enzymology 448:521–552. doi: 10.1016/S0076-6879(08)02626-8
    • (2008) Methods in Enzymology , vol.448 , pp. 521-552
    • Kedersha, N.1    Tisdale, S.2    Hickman, T.3    Erson, P.4
  • 26
    • 84862151933 scopus 로고    scopus 로고
    • The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease
    • King OD, Gitler AD, Shorter J. 2012. The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease. Brain Research 1462:61–80. doi: 10.1016/j.brainres.2012.01.016
    • (2012) Brain Research , vol.1462 , pp. 61-80
    • King, O.D.1    Gitler, A.D.2    Shorter, J.3
  • 27
    • 84940503517 scopus 로고    scopus 로고
    • Promiscuous interactions and protein disaggregases determine the material state of stress-inducible RNP granules
    • Kroschwald S, Maharana S, Mateju D, Malinovska L, Nüske E, Poser I, Richter D, Alberti S. 2015. Promiscuous interactions and protein disaggregases determine the material state of stress-inducible RNP granules. eLife 4: e06807. doi: 10.7554/eLife.06807
    • (2015) Elife , vol.4
    • Kroschwald, S.1    Maharana, S.2    Mateju, D.3    Malinovska, L.4    Nüske, E.5    Poser, I.6    Richter, D.7    Alberti, S.8
  • 28
  • 30
    • 84944884978 scopus 로고    scopus 로고
    • Formation and Maturation of Phase-Separated Liquid Droplets by RNA-Binding Proteins
    • Lin Y, Protter DS, Rosen MK, Parker R. 2015. Formation and Maturation of Phase-Separated Liquid Droplets by RNA-Binding Proteins. Molecular Cell 60:208–219. doi: 10.1016/j.molcel.2015.08.018
    • (2015) Molecular Cell , vol.60 , pp. 208-219
    • Lin, Y.1    Protter, D.S.2    Rosen, M.K.3    Parker, R.4
  • 32
    • 84944907005 scopus 로고    scopus 로고
    • Phase separation by low complexity domains promotesstre promotes stress granule assembly and drives pathological fibrillization
    • Molliex A, Temirov J, Lee J, Coughlin M, Kanagaraj AP, Kim HJ, Mittag T, Taylor JP. 2015. Phase separation by low complexity domains promotesstre promotes stress granule assembly and drives pathological fibrillization. Cell 163:123–133. doi: 10.1016/j.cell.2015.09.015
    • (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
  • 35
    • 53349165578 scopus 로고    scopus 로고
    • A functional RNAi screen links O-GlcNAc modification of ribosomal proteins to stress granule and processing body assembly
    • Ohn T, Kedersha N, Hickman T, Tisdale S, Anderson P. 2008. A functional RNAi screen links O-GlcNAc modification of ribosomal proteins to stress granule and processing body assembly. Nature Cell Biology 10: 1224–1231. doi: 10.1038/ncb1783
    • (2008) Nature Cell Biology , vol.10 , pp. 1224-1231
    • Ohn, T.1    Kedersha, N.2    Hickman, T.3    Tisdale, S.4    Erson, P.5
  • 38
    • 33947727395 scopus 로고    scopus 로고
    • Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex
    • Patel SS, Belmont BJ, Sante JM, Rexach MF. 2007. Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex. Cell 129:83–96. doi: 10.1016/j.cell.2007.01.044
    • (2007) Cell , vol.129 , pp. 83-96
    • Patel, S.S.1    Belmont, B.J.2    Sante, J.M.3    Rexach, M.F.4
  • 39
    • 84882801549 scopus 로고    scopus 로고
    • Altered ribostasis: RNA-protein granules in degenerative disorders
    • Ramaswami M, Taylor JP, Parker R. 2013. Altered ribostasis: RNA-protein granules in degenerative disorders. Cell 154:727–736. doi: 10.1016/j.cell.2013.07.038
    • (2013) Cell , vol.154 , pp. 727-736
    • Ramaswami, M.1    Taylor, J.P.2    Parker, R.3
  • 40
    • 50249131374 scopus 로고    scopus 로고
    • A role for Q/N-rich aggregation-prone regions in P-body localization
    • Reijns MA, Alexander RD, Spiller MP, Beggs JD. 2008. A role for Q/N-rich aggregation-prone regions in P-body localization. Journal of Cell Science 121:2463–2472. doi: 10.1242/jcs.024976
    • (2008) Journal of Cell Science , vol.121 , pp. 2463-2472
    • Reijns, M.A.1    Alexander, R.D.2    Spiller, M.P.3    Beggs, J.D.4
  • 41
    • 0037013954 scopus 로고    scopus 로고
    • The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion
    • Ribbeck K, Görlich D. 2002. The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion. The EMBO Journal 21:2664–2671. doi: 10.1093/emboj/21.11.2664
    • (2002) The EMBO Journal , vol.21 , pp. 2664-2671
    • Ribbeck, K.1    Görlich, D.2
  • 42
    • 84951794735 scopus 로고    scopus 로고
    • Transport Selectivity of Nuclear Pores, Phase Separation, and Membraneless Organelles
    • Schmidt HB, Görlich D. 2016. Transport Selectivity of Nuclear Pores, Phase Separation, and Membraneless Organelles. Trends in Biochemical Sciences 41:46–61. doi: 10.1016/j.tibs.2015.11.001
    • (2016) Trends in Biochemical Sciences , vol.41 , pp. 46-61
    • Schmidt, H.B.1    Görlich, D.2
  • 43
    • 84906877425 scopus 로고    scopus 로고
    • Assemblages: Functional units formed by cellular phase separation
    • Toretsky JA, Wright PE. 2014. Assemblages: functional units formed by cellular phase separation. The Journal of Cell Biology 206:579–588. doi: 10.1083/jcb.201404124
    • (2014) The Journal of Cell Biology , vol.206 , pp. 579-588
    • Toretsky, J.A.1    Wright, P.E.2
  • 44
    • 79955497151 scopus 로고    scopus 로고
    • P granules extend the nuclear pore complex environment in the C. Elegans germ line
    • Updike DL, Hachey SJ, Kreher J, Strome S. 2011. P granules extend the nuclear pore complex environment in the C. elegans germ line. The Journal of Cell Biology 192:939–948. doi: 10.1083/jcb.201010104
    • (2011) The Journal of Cell Biology , vol.192 , pp. 939-948
    • Updike, D.L.1    Hachey, S.J.2    Kreher, J.3    Strome, S.4
  • 46
    • 84939780690 scopus 로고    scopus 로고
    • Differential effects of Ydj1 and Sis1 on Hsp70-mediated clearance of stress granules in Saccharomyces cerevisiae
    • Walters RW, Muhlrad D, Garcia J, Parker R. 2015. Differential effects of Ydj1 and Sis1 on Hsp70-mediated clearance of stress granules in Saccharomyces cerevisiae. RNA 21:1660–1671. doi: 10.1261/rna.053116.115
    • (2015) RNA , vol.21 , pp. 1660-1671
    • Walters, R.W.1    Muhlrad, D.2    Garcia, J.3    Parker, R.4
  • 47
    • 84861964894 scopus 로고    scopus 로고
    • Getting RNA and protein in phase
    • Weber SC, Brangwynne CP. 2012. Getting RNA and protein in phase. Cell 149:1188–1191. doi: 10.1016/j.cell.2012.05.022
    • (2012) Cell , vol.149 , pp. 1188-1191
    • Weber, S.C.1    Brangwynne, C.P.2
  • 48
    • 84925114160 scopus 로고    scopus 로고
    • Intrinsically disordered proteins in cellular signalling and regulation
    • Wright PE, Dyson HJ. 2015. Intrinsically disordered proteins in cellular signalling and regulation. Nature Reviews Molecular Cell Biology 16:18–29. doi: 10.1038/nrm3920
    • (2015) Nature Reviews Molecular Cell Biology , vol.16 , pp. 18-29
    • Wright, P.E.1    Dyson, H.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.