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Volumn 10, Issue 11, 2014, Pages

Stress Granule-Defective Mutants Deregulate Stress Responsive Transcripts

Author keywords

[No Author keywords available]

Indexed keywords

GUANOSINE TRIPHOSPHATASE; MESSENGER RNA; RAN PROTEIN; RNA BINDING PROTEIN; GLUCOSE;

EID: 84912083665     PISSN: 15537390     EISSN: 15537404     Source Type: Journal    
DOI: 10.1371/journal.pgen.1004763     Document Type: Article
Times cited : (37)

References (74)
  • 1
    • 2942561052 scopus 로고    scopus 로고
    • Genome-wide analysis of mRNA stability using transcription inhibitors and microarrays reveals posttranscriptional control of ribosome biogenesis factors
    • Grigull J, Mnaimneh S, Pootoolal J, Robinson MD, Hughes TR, (2004) Genome-wide analysis of mRNA stability using transcription inhibitors and microarrays reveals posttranscriptional control of ribosome biogenesis factors. Mol Cell Biol 24: 5534–5547.
    • (2004) Mol Cell Biol , vol.24 , pp. 5534-5547
    • Grigull, J.1    Mnaimneh, S.2    Pootoolal, J.3    Robinson, M.D.4    Hughes, T.R.5
  • 2
    • 62549149882 scopus 로고    scopus 로고
    • MRNA stability changes precede changes in steady-state mRNA amounts during hyperosmotic stress
    • Molin C, Jauhiainen A, Warringer J, Nerman O, Sunnerhagen P, (2009) mRNA stability changes precede changes in steady-state mRNA amounts during hyperosmotic stress. RNA 15: 600–614.
    • (2009) RNA , vol.15 , pp. 600-614
    • Molin, C.1    Jauhiainen, A.2    Warringer, J.3    Nerman, O.4    Sunnerhagen, P.5
  • 3
    • 66449128185 scopus 로고    scopus 로고
    • Specific and global regulation of mRNA stability during osmotic stress in Saccharomyces cerevisiae
    • Romero-Santacreu L, Moreno J, Pérez-Ortín JE, Alepuz P, (2009) Specific and global regulation of mRNA stability during osmotic stress in Saccharomyces cerevisiae. RNA 15: 1110–1120.
    • (2009) RNA , vol.15 , pp. 1110-1120
    • Romero-Santacreu, L.1    Moreno, J.2    Pérez-Ortín, J.E.3    Alepuz, P.4
  • 4
    • 77956235998 scopus 로고    scopus 로고
    • The HOG pathway dictates the short-term translational response after hyperosmotic shock
    • Warringer J, Hult M, Regot S, Posas F, Sunnerhagen P, (2010) The HOG pathway dictates the short-term translational response after hyperosmotic shock. Mol Biol Cell 21: 3080–3092.
    • (2010) Mol Biol Cell , vol.21 , pp. 3080-3092
    • Warringer, J.1    Hult, M.2    Regot, S.3    Posas, F.4    Sunnerhagen, P.5
  • 5
    • 45749090082 scopus 로고    scopus 로고
    • Yeast translational response to high salinity: Global analysis reveals regulation at multiple levels
    • Melamed D, Pnueli L, Arava Y, (2008) Yeast translational response to high salinity: Global analysis reveals regulation at multiple levels. RNA 14: 1337–1351.
    • (2008) RNA , vol.14 , pp. 1337-1351
    • Melamed, D.1    Pnueli, L.2    Arava, Y.3
  • 6
    • 33749379882 scopus 로고    scopus 로고
    • Global translational responses to oxidative stress impact upon multiple levels of protein synthesis
    • Shenton D, Smirnova JB, Selley JN, Carroll K, Hubbard SJ, et al. (2006) Global translational responses to oxidative stress impact upon multiple levels of protein synthesis. J Biol Chem 281: 29011–29021.
    • (2006) J Biol Chem , vol.281 , pp. 29011-29021
    • Shenton, D.1    Smirnova, J.B.2    Selley, J.N.3    Carroll, K.4    Hubbard, S.J.5
  • 7
    • 84855379287 scopus 로고    scopus 로고
    • The yeast mRNA cap-binding protein Cbc1/Sto1 is necessary for rapid reprogramming of translation after hyperosmotic shock
    • Garre E, Romero-Santacreu L, De Clercq N, Blasco N, Sunnerhagen P, et al. (2012) The yeast mRNA cap-binding protein Cbc1/Sto1 is necessary for rapid reprogramming of translation after hyperosmotic shock. Mol Biol Cell 23: 137–150.
    • (2012) Mol Biol Cell , vol.23 , pp. 137-150
    • Garre, E.1    Romero-Santacreu, L.2    De Clercq, N.3    Blasco, N.4    Sunnerhagen, P.5
  • 8
    • 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 Biochem Sci 38: 494–506.
    • (2013) Trends Biochem Sci , vol.38 , pp. 494-506
    • Kedersha, N.1    Ivanov, P.2    Anderson, P.3
  • 9
    • 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. Mol Cell 36: 932–941.
    • (2009) Mol Cell , vol.36 , pp. 932-941
    • Buchan, J.R.1    Parker, R.2
  • 10
    • 39949085583 scopus 로고    scopus 로고
    • Stress granules: the Tao of RNA triage
    • Anderson P, 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
  • 11
    • 56149086182 scopus 로고    scopus 로고
    • P bodies promote stress granule assembly in Saccharomyces cerevisiae
    • Buchan JR, Muhlrad D, Parker R, (2008) P bodies promote stress granule assembly in Saccharomyces cerevisiae. J Cell Biol 183: 441–455.
    • (2008) J Cell Biol , vol.183 , pp. 441-455
    • Buchan, J.R.1    Muhlrad, D.2    Parker, R.3
  • 12
    • 84871744570 scopus 로고    scopus 로고
    • Processing body and stress granule assembly occur by independent and differentially regulated pathways in Saccharomyces cerevisiae
    • Shah KH, Zhang B, Ramachandran V, Herman PK, (2013) Processing body and stress granule assembly occur by independent and differentially regulated pathways in Saccharomyces cerevisiae. Genetics 193: 109–123.
    • (2013) Genetics , vol.193 , pp. 109-123
    • Shah, K.H.1    Zhang, B.2    Ramachandran, V.3    Herman, P.K.4
  • 13
    • 35348989809 scopus 로고    scopus 로고
    • Stress-dependent relocalization of translationally primed mRNPs to cytoplasmic granules that are kinetically and spatially distinct from P-bodies
    • Hoyle NP, Castelli LM, Campbell SG, Holmes LE, Ashe MP, (2007) Stress-dependent relocalization of translationally primed mRNPs to cytoplasmic granules that are kinetically and spatially distinct from P-bodies. J Cell Biol 179: 65–74.
    • (2007) J Cell Biol , vol.179 , pp. 65-74
    • Hoyle, N.P.1    Castelli, L.M.2    Campbell, S.G.3    Holmes, L.E.4    Ashe, M.P.5
  • 14
    • 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. Nat Cell Biol 10: 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
  • 15
    • 84864308260 scopus 로고    scopus 로고
    • Transient sequestration of TORC1 into stress granules during heat stress
    • Takahara T, Maeda T, (2012) Transient sequestration of TORC1 into stress granules during heat stress. Mol Cell 47: 242–252.
    • (2012) Mol Cell , vol.47 , pp. 242-252
    • Takahara, T.1    Maeda, T.2
  • 16
    • 55549130760 scopus 로고    scopus 로고
    • Formation of stress granules inhibits apoptosis by suppressing stress-responsive MAPK pathways
    • Arimoto K, Fukuda H, Imajoh-Ohmi S, Saito H, Takekawa M, (2008) Formation of stress granules inhibits apoptosis by suppressing stress-responsive MAPK pathways. Nat Cell Biol 10: 1324–1332.
    • (2008) Nat Cell Biol , vol.10 , pp. 1324-1332
    • Arimoto, K.1    Fukuda, H.2    Imajoh-Ohmi, S.3    Saito, H.4    Takekawa, M.5
  • 17
    • 84873862712 scopus 로고    scopus 로고
    • Stress granules inhibit apoptosis by reducing reactive oxygen species production
    • Takahashi M, Higuchi M, Matsuki H, Yoshita M, Ohsawa T, et al. (2012) Stress granules inhibit apoptosis by reducing reactive oxygen species production. Mol Cell Biol 33: 815–829.
    • (2012) Mol Cell Biol , vol.33 , pp. 815-829
    • Takahashi, M.1    Higuchi, M.2    Matsuki, H.3    Yoshita, M.4    Ohsawa, T.5
  • 18
    • 84863383030 scopus 로고    scopus 로고
    • Analysis of stress granule assembly in Schizosaccharomyces pombe
    • Wang C-Y, Wen W-L, Nilsson D, Sunnerhagen P, Chang T-H, et al. (2012) Analysis of stress granule assembly in Schizosaccharomyces pombe. RNA 18: 694–703.
    • (2012) RNA , vol.18 , pp. 694-703
    • Wang, C.-Y.1    Wen, W.-L.2    Nilsson, D.3    Sunnerhagen, P.4    Chang, T.-H.5
  • 19
    • 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.
    • (2013) Cell , vol.154 , pp. 727-736
    • Ramaswami, M.1    Taylor, J.P.2    Parker, R.3
  • 20
    • 63049130206 scopus 로고    scopus 로고
    • Cells lacking the fragile X mental retardation protein (FMRP) have normal RISC activity but exhibit altered stress granule assembly
    • Didiot MC, Subramanian M, Flatter E, Mandel JL, Moine H, (2009) Cells lacking the fragile X mental retardation protein (FMRP) have normal RISC activity but exhibit altered stress granule assembly. Mol Biol Cell 20: 428–437.
    • (2009) Mol Biol Cell , vol.20 , pp. 428-437
    • Didiot, M.C.1    Subramanian, M.2    Flatter, E.3    Mandel, J.L.4    Moine, H.5
  • 21
    • 0033611157 scopus 로고    scopus 로고
    • RNA-binding proteins TIA-1 and TIAR link the phosphorylation of eIF-2 alpha to the assembly of mammalian stress granules
    • Kedersha NL, Gupta M, Li W, Miller I, Anderson P, (1999) RNA-binding proteins TIA-1 and TIAR link the phosphorylation of eIF-2 alpha to the assembly of mammalian stress granules. J Cell Biol 147: 1431–1442.
    • (1999) J Cell Biol , vol.147 , pp. 1431-1442
    • Kedersha, N.L.1    Gupta, M.2    Li, W.3    Miller, I.4    Anderson, P.5
  • 22
    • 68949172267 scopus 로고    scopus 로고
    • Robust heat shock induces eIF2alpha-phosphorylation-independent assembly of stress granules containing eIF3 and 40S ribosomal subunits in budding yeast, Saccharomyces cerevisiae
    • Grousl T, Ivanov P, Frydlova I, Vasicova P, Janda F, et al. (2009) Robust heat shock induces eIF2alpha-phosphorylation-independent assembly of stress granules containing eIF3 and 40S ribosomal subunits in budding yeast, Saccharomyces cerevisiae. J Cell Sci 122: 2078–2088.
    • (2009) J Cell Sci , vol.122 , pp. 2078-2088
    • Grousl, T.1    Ivanov, P.2    Frydlova, I.3    Vasicova, P.4    Janda, F.5
  • 23
    • 78049392024 scopus 로고    scopus 로고
    • Vgl1, a multi-KH domain protein, is a novel component of the fission yeast stress granules required for cell survival under thermal stress
    • Wen WL, Stevenson AL, Wang CY, Chen HJ, Kearsey SE, et al. (2010) Vgl1, a multi-KH domain protein, is a novel component of the fission yeast stress granules required for cell survival under thermal stress. Nucleic Acids Res 38: 6555–6566.
    • (2010) Nucleic Acids Res , vol.38 , pp. 6555-6566
    • Wen, W.L.1    Stevenson, A.L.2    Wang, C.Y.3    Chen, H.J.4    Kearsey, S.E.5
  • 24
    • 78650499705 scopus 로고    scopus 로고
    • Cellular stress induces cytoplasmic RNA granules in fission yeast
    • Nilsson D, Sunnerhagen P, (2011) Cellular stress induces cytoplasmic RNA granules in fission yeast. RNA 17: 120–133.
    • (2011) RNA , vol.17 , pp. 120-133
    • Nilsson, D.1    Sunnerhagen, P.2
  • 25
    • 79251554956 scopus 로고    scopus 로고
    • Stress-specific composition, assembly and kinetics of stress granules in Saccharomyces cerevisiae
    • Buchan JR, Yoon JH, Parker R, (2011) Stress-specific composition, assembly and kinetics of stress granules in Saccharomyces cerevisiae. J Cell Sci 124: 228–239.
    • (2011) J Cell Sci , vol.124 , pp. 228-239
    • Buchan, J.R.1    Yoon, J.H.2    Parker, R.3
  • 26
    • 84874514535 scopus 로고    scopus 로고
    • Heat shock-induced accumulation of translation elongation and termination factors precedes assembly of stress granules in S. cerevisiae
    • Grousl T, Ivanov P, Malcova I, Pompach P, Frydlova I, et al. (2013) Heat shock-induced accumulation of translation elongation and termination factors precedes assembly of stress granules in S. cerevisiae. PLoS One 8: e57083.
    • (2013) PLoS One , vol.8 , pp. e57083
    • Grousl, T.1    Ivanov, P.2    Malcova, I.3    Pompach, P.4    Frydlova, I.5
  • 27
    • 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.
    • (2013) Cell , vol.153 , pp. 1461-1474
    • Buchan, J.R.1    Kolaitis, R.M.2    Taylor, J.P.3    Parker, R.4
  • 28
    • 21244448694 scopus 로고    scopus 로고
    • The TOR and EGO protein complexes orchestrate microautophagy in yeast
    • Dubouloz F, Deloche O, Wanke V, Cameroni E, De Virgilio C, (2005) The TOR and EGO protein complexes orchestrate microautophagy in yeast. Mol Cell 19: 15–26.
    • (2005) Mol Cell , vol.19 , pp. 15-26
    • Dubouloz, F.1    Deloche, O.2    Wanke, V.3    Cameroni, E.4    De Virgilio, C.5
  • 29
    • 0034638837 scopus 로고    scopus 로고
    • Dynamic shuttling of TIA-1 accompanies the recruitment of mRNA to mammalian stress granules
    • Kedersha N, Cho MR, Li W, Yacono PW, Chen S, et al. (2000) Dynamic shuttling of TIA-1 accompanies the recruitment of mRNA to mammalian stress granules. J Cell Biol 151: 1257–1268.
    • (2000) J Cell Biol , vol.151 , pp. 1257-1268
    • Kedersha, N.1    Cho, M.R.2    Li, W.3    Yacono, P.W.4    Chen, S.5
  • 30
    • 0037968357 scopus 로고    scopus 로고
    • Decapping and decay of messenger RNA occur in cytoplasmic processing bodies
    • Sheth U, Parker R, (2003) Decapping and decay of messenger RNA occur in cytoplasmic processing bodies. Science 300: 805–808.
    • (2003) Science , vol.300 , pp. 805-808
    • Sheth, U.1    Parker, R.2
  • 31
    • 84860872161 scopus 로고    scopus 로고
    • Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels
    • Kato M, Han TW, Xie S, Shi K, Du X, 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
  • 32
    • 33845358661 scopus 로고    scopus 로고
    • A novel algorithm for identifying low-complexity regions in a protein sequence
    • Li X, Kahveci T, (2006) A novel algorithm for identifying low-complexity regions in a protein sequence. Bioinformatics 22: 2980–2987.
    • (2006) Bioinformatics , vol.22 , pp. 2980-2987
    • Li, X.1    Kahveci, T.2
  • 33
    • 84876288161 scopus 로고    scopus 로고
    • Protein disorder, prion propensities, and self-organizing macromolecular collectives
    • Malinovska L, Kroschwald S, Alberti S, (2013) Protein disorder, prion propensities, and self-organizing macromolecular collectives. Biochim Biophys Acta 1834: 918–31.
    • (2013) Biochim Biophys Acta , vol.1834 , pp. 918-931
    • Malinovska, L.1    Kroschwald, S.2    Alberti, S.3
  • 34
    • 67049119327 scopus 로고    scopus 로고
    • Prediction of protein binding regions in disordered proteins
    • Meszaros B, Simon I, Dosztanyi Z, (2009) Prediction of protein binding regions in disordered proteins. PLoS Comput Biol 5: e1000376.
    • (2009) PLoS Comput Biol , vol.5 , pp. e1000376
    • Meszaros, B.1    Simon, I.2    Dosztanyi, Z.3
  • 36
    • 0034936969 scopus 로고    scopus 로고
    • Cytotoxic and genotoxic consequences of heat stress are dependent on the presence of oxygen in Saccharomyces cerevisiae
    • Davidson JF, Schiestl RH, (2001) Cytotoxic and genotoxic consequences of heat stress are dependent on the presence of oxygen in Saccharomyces cerevisiae. J Bacteriol 183: 4580–4587.
    • (2001) J Bacteriol , vol.183 , pp. 4580-4587
    • Davidson, J.F.1    Schiestl, R.H.2
  • 38
    • 79953845487 scopus 로고    scopus 로고
    • Systematic exploration of essential yeast gene function with temperature-sensitive mutants
    • Li Z, Vizeacoumar FJ, Bahr S, Li J, Warringer J, et al. (2011) Systematic exploration of essential yeast gene function with temperature-sensitive mutants. Nat Biotechnol 29: 361–367.
    • (2011) Nat Biotechnol , vol.29 , pp. 361-367
    • Li, Z.1    Vizeacoumar, F.J.2    Bahr, S.3    Li, J.4    Warringer, J.5
  • 39
    • 84873665112 scopus 로고    scopus 로고
    • Regulation of mTORC1 by the Rag GTPases is necessary for neonatal autophagy and survival
    • Efeyan A, Zoncu R, Chang S, Gumper I, Snitkin H, et al. (2013) Regulation of mTORC1 by the Rag GTPases is necessary for neonatal autophagy and survival. Nature 493: 679–683.
    • (2013) Nature , vol.493 , pp. 679-683
    • Efeyan, A.1    Zoncu, R.2    Chang, S.3    Gumper, I.4    Snitkin, H.5
  • 40
    • 77149120760 scopus 로고    scopus 로고
    • Differential localization to cytoplasm, nucleus or P-bodies of yeast PKA subunits under different growth conditions
    • Tudisca V, Recouvreux V, Moreno S, Boy-Marcotte E, Jacquet M, et al. (2010) Differential localization to cytoplasm, nucleus or P-bodies of yeast PKA subunits under different growth conditions. Eur J Cell Biol 89: 339–348.
    • (2010) Eur J Cell Biol , vol.89 , pp. 339-348
    • Tudisca, V.1    Recouvreux, V.2    Moreno, S.3    Boy-Marcotte, E.4    Jacquet, M.5
  • 41
    • 77956006894 scopus 로고    scopus 로고
    • Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function
    • Welker S, Rudolph B, Frenzel E, Hagn F, Liebisch G, et al. (2010) Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function. Mol Cell 39: 507–520.
    • (2010) Mol Cell , vol.39 , pp. 507-520
    • Welker, S.1    Rudolph, B.2    Frenzel, E.3    Hagn, F.4    Liebisch, G.5
  • 42
    • 5444256434 scopus 로고    scopus 로고
    • A dynamic transcriptional network communicates growth potential to ribosome synthesis and critical cell size
    • Jorgensen P, Rupes I, Sharom JR, Schneper L, Broach JR, et al. (2004) A dynamic transcriptional network communicates growth potential to ribosome synthesis and critical cell size. Genes Dev 18: 2491–2505.
    • (2004) Genes Dev , vol.18 , pp. 2491-2505
    • Jorgensen, P.1    Rupes, I.2    Sharom, J.R.3    Schneper, L.4    Broach, J.R.5
  • 43
    • 34249813098 scopus 로고    scopus 로고
    • Sch9 is a major target of TORC1 in Saccharomyces cerevisiae
    • Urban J, Soulard A, Huber A, Lippman S, Mukhopadhyay D, et al. (2007) Sch9 is a major target of TORC1 in Saccharomyces cerevisiae. Mol Cell 26: 663–674.
    • (2007) Mol Cell , vol.26 , pp. 663-674
    • Urban, J.1    Soulard, A.2    Huber, A.3    Lippman, S.4    Mukhopadhyay, D.5
  • 44
    • 0036282743 scopus 로고    scopus 로고
    • Osmotic stress signaling and osmoadaptation in yeasts
    • Hohmann S, (2002) Osmotic stress signaling and osmoadaptation in yeasts. Microbiol Mol Biol Rev 66: 300–372.
    • (2002) Microbiol Mol Biol Rev , vol.66 , pp. 300-372
    • Hohmann, S.1
  • 45
    • 0037382865 scopus 로고    scopus 로고
    • Translational control by TOR and TAP42 through dephosphorylation of eIF2alpha kinase GCN2
    • Cherkasova VA, Hinnebusch AG, (2003) Translational control by TOR and TAP42 through dephosphorylation of eIF2alpha kinase GCN2. Genes Dev 17: 859–872.
    • (2003) Genes Dev , vol.17 , pp. 859-872
    • Cherkasova, V.A.1    Hinnebusch, A.G.2
  • 47
    • 77957867303 scopus 로고    scopus 로고
    • Mutant FUS proteins that cause amyotrophic lateral sclerosis incorporate into stress granules
    • Bosco DA, Lemay N, Ko HK, Zhou H, Burke C, et al. (2010) Mutant FUS proteins that cause amyotrophic lateral sclerosis incorporate into stress granules. Hum Mol Genet 19: 4160–4175.
    • (2010) Hum Mol Genet , vol.19 , pp. 4160-4175
    • Bosco, D.A.1    Lemay, N.2    Ko, H.K.3    Zhou, H.4    Burke, C.5
  • 48
    • 82355171757 scopus 로고    scopus 로고
    • A novel origin for granulovacuolar degeneration in aging and Alzheimer's disease: parallels to stress granules
    • Castellani RJ, Gupta Y, Sheng B, Siedlak SL, Harris PL, et al. (2011) A novel origin for granulovacuolar degeneration in aging and Alzheimer's disease: parallels to stress granules. Lab Invest 91: 1777–1786.
    • (2011) Lab Invest , vol.91 , pp. 1777-1786
    • Castellani, R.J.1    Gupta, Y.2    Sheng, B.3    Siedlak, S.L.4    Harris, P.L.5
  • 49
    • 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, et al. (2012) Cell-free formation of RNA granules: bound RNAs identify features and components of cellular assemblies. Cell 149: 768–779.
    • (2012) Cell , vol.149 , pp. 768-779
    • Han, T.W.1    Kato, M.2    Xie, S.3    Wu, L.C.4    Mirzaei, H.5
  • 50
    • 0028849086 scopus 로고
    • Cloning of a novel family of mammalian GTP-binding proteins (RagA, RagBs, RagB1) with remote similarity to the Ras-related GTPases
    • Schürmann A, Brauers A, Massmann S, Becker W, Joost HG, (1995) Cloning of a novel family of mammalian GTP-binding proteins (RagA, RagBs, RagB1) with remote similarity to the Ras-related GTPases. J Biol Chem 270: 28982–28988.
    • (1995) J Biol Chem , vol.270 , pp. 28982-28988
    • Schürmann, A.1    Brauers, A.2    Massmann, S.3    Becker, W.4    Joost, H.G.5
  • 51
    • 0029811390 scopus 로고    scopus 로고
    • Putative GTPase Gtr1p genetically interacts with the RanGTPase cycle in Saccharomyces cerevisiae
    • Nakashima N, Hayashi N, Noguchi E, Nishimoto T, (1996) Putative GTPase Gtr1p genetically interacts with the RanGTPase cycle in Saccharomyces cerevisiae. J Cell Sci 109: 2311–2318.
    • (1996) J Cell Sci , vol.109 , pp. 2311-2318
    • Nakashima, N.1    Hayashi, N.2    Noguchi, E.3    Nishimoto, T.4
  • 52
    • 33745745910 scopus 로고    scopus 로고
    • A conserved GTPase-containing complex is required for intracellular sorting of the general amino-acid permease in yeast
    • Gao M, Kaiser CA, (2006) A conserved GTPase-containing complex is required for intracellular sorting of the general amino-acid permease in yeast. Nat Cell Biol 8: 657–667.
    • (2006) Nat Cell Biol , vol.8 , pp. 657-667
    • Gao, M.1    Kaiser, C.A.2
  • 53
    • 45849105156 scopus 로고    scopus 로고
    • The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1
    • Sancak Y, Peterson TR, Shaul YD, Lindquist RA, Thoreen CC, et al. (2008) The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1. Science 320: 1496–1501.
    • (2008) Science , vol.320 , pp. 1496-1501
    • Sancak, Y.1    Peterson, T.R.2    Shaul, Y.D.3    Lindquist, R.A.4    Thoreen, C.C.5
  • 54
    • 39749156312 scopus 로고    scopus 로고
    • Genetic evidence that Ras-like GTPases, Gtr1p, and Gtr2p, are involved in epigenetic control of gene expression in Saccharomyces cerevisiae
    • Sekiguchi T, Hayashi N, Wang Y, Kobayashi H, (2008) Genetic evidence that Ras-like GTPases, Gtr1p, and Gtr2p, are involved in epigenetic control of gene expression in Saccharomyces cerevisiae. Biochem Biophys Res Commun 368: 748–754.
    • (2008) Biochem Biophys Res Commun , vol.368 , pp. 748-754
    • Sekiguchi, T.1    Hayashi, N.2    Wang, Y.3    Kobayashi, H.4
  • 55
    • 33750472331 scopus 로고    scopus 로고
    • Ltv1 is required for efficient nuclear export of the ribosomal small subunit in Saccharomyces cerevisiae
    • Seiser RM, Sundberg AE, Wollam BJ, Zobel-Thropp P, Baldwin K, et al. (2006) Ltv1 is required for efficient nuclear export of the ribosomal small subunit in Saccharomyces cerevisiae. Genetics 174: 679–691.
    • (2006) Genetics , vol.174 , pp. 679-691
    • Seiser, R.M.1    Sundberg, A.E.2    Wollam, B.J.3    Zobel-Thropp, P.4    Baldwin, K.5
  • 56
    • 25444456114 scopus 로고    scopus 로고
    • Association of the GTP-binding protein Gtr1p with Rpc19p, a shared subunit of RNA polymerase I and III in yeast Saccharomyces cerevisiae
    • Todaka Y, Wang Y, Tashiro K, Nakashima N, Nishimoto T, et al. (2005) Association of the GTP-binding protein Gtr1p with Rpc19p, a shared subunit of RNA polymerase I and III in yeast Saccharomyces cerevisiae. Genetics 170: 1515–1524.
    • (2005) Genetics , vol.170 , pp. 1515-1524
    • Todaka, Y.1    Wang, Y.2    Tashiro, K.3    Nakashima, N.4    Nishimoto, T.5
  • 57
    • 84879515784 scopus 로고    scopus 로고
    • Identification of novel stress granule components that are involved in nuclear transport
    • Mahboubi H, Seganathy E, Kong D, Stochaj U, (2013) Identification of novel stress granule components that are involved in nuclear transport. PLoS One 8: e68356.
    • (2013) PLoS One , vol.8 , pp. e68356
    • Mahboubi, H.1    Seganathy, E.2    Kong, D.3    Stochaj, U.4
  • 58
    • 84871675341 scopus 로고    scopus 로고
    • Nuclear import of UBL-domain protein Mdy2 is required for heat-induced stress response in Saccharomyces cerevisiae
    • Arhzaouy K, Ramezani-Rad M, (2012) Nuclear import of UBL-domain protein Mdy2 is required for heat-induced stress response in Saccharomyces cerevisiae. PLoS One 7: e52956.
    • (2012) PLoS One , vol.7 , pp. e52956
    • Arhzaouy, K.1    Ramezani-Rad, M.2
  • 59
    • 84878270249 scopus 로고    scopus 로고
    • Gene expression is circular: factors for mRNA degradation also foster mRNA synthesis
    • Haimovich G, Medina DA, Causse SZ, Garber M, Millan-Zambrano G, et al. (2013) Gene expression is circular: factors for mRNA degradation also foster mRNA synthesis. Cell 153: 1000–1011.
    • (2013) Cell , vol.153 , pp. 1000-1011
    • Haimovich, G.1    Medina, D.A.2    Causse, S.Z.3    Garber, M.4    Millan-Zambrano, G.5
  • 60
    • 84866426158 scopus 로고    scopus 로고
    • Large G3BP-induced granules trigger eIF2alpha phosphorylation
    • Reineke LC, Dougherty JD, Pierre P, Lloyd RE, (2012) Large G3BP-induced granules trigger eIF2alpha phosphorylation. Mol Biol Cell 23: 3499–3510.
    • (2012) Mol Biol Cell , vol.23 , pp. 3499-3510
    • Reineke, L.C.1    Dougherty, J.D.2    Pierre, P.3    Lloyd, R.E.4
  • 61
    • 0035937098 scopus 로고    scopus 로고
    • Arc1p organizes the yeast aminoacyl-tRNA synthetase complex and stabilizes its interaction with the cognate tRNAs
    • Deinert K, Fasiolo F, Hurt EC, Simos G, (2001) Arc1p organizes the yeast aminoacyl-tRNA synthetase complex and stabilizes its interaction with the cognate tRNAs. J Biol Chem 276: 6000–6008.
    • (2001) J Biol Chem , vol.276 , pp. 6000-6008
    • Deinert, K.1    Fasiolo, F.2    Hurt, E.C.3    Simos, G.4
  • 62
    • 65249129859 scopus 로고    scopus 로고
    • Angiogenin cleaves tRNA and promotes stress-induced translational repression
    • Yamasaki S, Ivanov P, Hu GF, Anderson P, (2009) Angiogenin cleaves tRNA and promotes stress-induced translational repression. J Cell Biol 185: 35–42.
    • (2009) J Cell Biol , vol.185 , pp. 35-42
    • Yamasaki, S.1    Ivanov, P.2    Hu, G.F.3    Anderson, P.4
  • 63
    • 0035861532 scopus 로고    scopus 로고
    • Systematic genetic analysis with ordered arrays of yeast deletion mutants
    • Tong AH, Evangelista M, Parsons AB, Xu H, Bader GD, et al. (2001) Systematic genetic analysis with ordered arrays of yeast deletion mutants. Science 294: 2364–2368.
    • (2001) Science , vol.294 , pp. 2364-2368
    • Tong, A.H.1    Evangelista, M.2    Parsons, A.B.3    Xu, H.4    Bader, G.D.5
  • 64
    • 10744230485 scopus 로고    scopus 로고
    • Global mapping of the yeast genetic interaction network
    • Tong AH, Lesage G, Bader GD, Ding H, Xu H, et al. (2004) Global mapping of the yeast genetic interaction network. Science 303: 808–813.
    • (2004) Science , vol.303 , pp. 808-813
    • Tong, A.H.1    Lesage, G.2    Bader, G.D.3    Ding, H.4    Xu, H.5
  • 65
    • 64349112353 scopus 로고    scopus 로고
    • A molecular barcoded yeast ORF library enables mode-of-action analysis of bioactive compounds
    • Ho CH, Magtanong L, Barker SL, Gresham D, Nishimura S, et al. (2009) A molecular barcoded yeast ORF library enables mode-of-action analysis of bioactive compounds. Nat Biotechnol 27: 369–377.
    • (2009) Nat Biotechnol , vol.27 , pp. 369-377
    • Ho, C.H.1    Magtanong, L.2    Barker, S.L.3    Gresham, D.4    Nishimura, S.5
  • 66
    • 12344269924 scopus 로고    scopus 로고
    • GO Term Finder - open source software for accessing Gene Ontology information and finding significantly enriched Gene Ontology terms associated with a list of genes
    • Boyle EI, Weng S, Gollub J, Jin H, Botstein D, et al. (2004) GO Term Finder - open source software for accessing Gene Ontology information and finding significantly enriched Gene Ontology terms associated with a list of genes. Bioinformatics 20: 3710–3715.
    • (2004) Bioinformatics , vol.20 , pp. 3710-3715
    • Boyle, E.I.1    Weng, S.2    Gollub, J.3    Jin, H.4    Botstein, D.5
  • 71
    • 0037438569 scopus 로고    scopus 로고
    • Automated screening in environmental arrays allows analysis of quantitative phenotypic profiles in Saccharomyces cerevisiae
    • Warringer J, Blomberg A, (2003) Automated screening in environmental arrays allows analysis of quantitative phenotypic profiles in Saccharomyces cerevisiae. Yeast 20: 53–67.
    • (2003) Yeast , vol.20 , pp. 53-67
    • Warringer, J.1    Blomberg, A.2
  • 72
    • 0018403943 scopus 로고
    • Expression of radiation-induced mutations at the arginine permease (CAN1) locus in Saccharomyces cerevisiae
    • Gocke E, Manney TR, (1979) Expression of radiation-induced mutations at the arginine permease (CAN1) locus in Saccharomyces cerevisiae. Genetics 91: 53–66.
    • (1979) Genetics , vol.91 , pp. 53-66
    • Gocke, E.1    Manney, T.R.2
  • 73
  • 74
    • 33747191719 scopus 로고    scopus 로고
    • Prevalent structural disorder in E. coli and S. cerevisiae proteomes
    • Tompa P, Dosztanyi Z, Simon I, (2006) Prevalent structural disorder in E. coli and S. cerevisiae proteomes. J Proteome Res 5: 1996–2000.
    • (2006) J Proteome Res , vol.5 , pp. 1996-2000
    • Tompa, P.1    Dosztanyi, Z.2    Simon, I.3


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