메뉴 건너뛰기




Volumn 18, Issue 4, 2012, Pages 694-703

Analysis of stress granule assembly in Schizosaccharomyces pombe

Author keywords

Ataxia two homolog Ath1; Deubiquitinating protease Ubp3; Fission yeast stress granules; G3BP like protein Nxt3; TIA like proteins

Indexed keywords

ARTICLE; CELL GRANULE; FISSION YEAST STRESS GRANULE; HUMAN; MOLECULAR MECHANICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN INTERACTION; PROTEIN MODIFICATION; SCHIZOSACCHAROMYCES POMBE; TEMPERATURE STRESS;

EID: 84863383030     PISSN: 13558382     EISSN: 14699001     Source Type: Journal    
DOI: 10.1261/rna.030270.111     Document Type: Article
Times cited : (30)

References (34)
  • 1
    • 3242890363 scopus 로고    scopus 로고
    • Structural and functional analysis of ataxin-2 and ataxin-3
    • DOI 10.1111/j.1432-1033.2004.04245.x
    • Albrecht M, Golatta M, Wullner U, Lengauer T. 2004. Structural and functional analysis of ataxin-2 and ataxin-3. Eur J Biochem 271: 3155-3170. (Pubitemid 38998685)
    • (2004) European Journal of Biochemistry , vol.271 , Issue.15 , pp. 3155-3170
    • Albrecht, M.1    Golatta, M.2    Wullner, U.3    Lengauer, T.4
  • 2
    • 66249103703 scopus 로고    scopus 로고
    • RNA granules: Post-transcriptional and epigenetic modulators of gene expression
    • Anderson P, Kedersha N. 2009. RNA granules: Post-transcriptional and epigenetic modulators of gene expression. Nat Rev Mol Cell Biol 10: 430-436.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 430-436
    • Anderson, P.1    Kedersha, N.2
  • 3
    • 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
  • 4
    • 33846162752 scopus 로고    scopus 로고
    • Dynamic association with polysomes during P19 neuronal differentiation and an untranslated-region-dependent translation regulation of the tau mRNA by the tau mRNA-associated proteins IMP1, HuD, and G3BP1
    • DOI 10.1002/jnr.21099
    • Atlas R, Behar L, Sapoznik S, Ginzburg I. 2007. Dynamic association with polysomes during P19 neuronal differentiation and an untranslated- region-dependent translation regulation of the tau mRNA by the tau mRNA-associated proteins IMP1, HuD, and G3BP1. J Neurosci Res 85: 173-183. (Pubitemid 46079807)
    • (2007) Journal of Neuroscience Research , vol.85 , Issue.1 , pp. 173-183
    • Atlas, R.1    Behar, L.2    Sapoznik, S.3    Ginzburg, I.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. Mol Cell 36: 932-941.
    • (2009) Mol Cell , vol.36 , pp. 932-941
    • Buchan, J.R.1    Parker, R.2
  • 6
    • 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
  • 7
    • 0038387865 scopus 로고    scopus 로고
    • Ubp3 requires a cofactor, Bre5, to specifically de-ubiquitinate the COPII protein, Sec23
    • DOI 10.1038/ncb1003
    • Cohen M, Stutz F, Belgareh N, Haguenauer-Tsapis R, Dargemont C. 2003. Ubp3 requires a cofactor, Bre5, to specifically de-ubiquitinate the COPII protein, Sec23. Nat Cell Biol 5: 661-667. (Pubitemid 36818089)
    • (2003) Nature Cell Biology , vol.5 , Issue.7 , pp. 661-667
    • Cohen, M.1    Stutz, F.2    Belgareh, N.3    Haguenauer-Tsapis, R.4    Dargemont, C.5
  • 8
    • 33845950751 scopus 로고    scopus 로고
    • Eukaryotic initiation factor 2a-independent pathway of stress granule induction by the natural product pateamine A
    • DOI 10.1074/jbc.M606149200
    • Dang Y, Kedersha N, Low WK, Romo D, Gorospe M, Kaufman R, Anderson P, Liu JO. 2006. Eukaryotic initiation factor 2a-independent pathway of stress granule induction by the natural product pateamine A. J Biol Chem 281: 32870-32878. (Pubitemid 46036842)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.43 , pp. 32870-32878
    • Dang, Y.1    Kedersha, N.2    Low, W.-K.3    Romo, D.4    Gorospe, M.5    Kaufman, R.6    Anderson, P.7    Liu, J.O.8
  • 9
    • 36049032156 scopus 로고    scopus 로고
    • The cold-inducible RNA-binding protein migrates from the nucleus to cytoplasmic stress granules by a methylation-dependent mechanism and acts as a translational repressor
    • DOI 10.1016/j.yexcr.2007.09.017, PII S001448270700451X
    • De Leeuw F, Zhang T, Wauquier C, Huez G, Kruys V, Gueydan C. 2007. The cold-inducible RNA-binding protein migrates from the nucleus to cytoplasmic stress granules by a methylation-dependent mechanism and acts as a translational repressor. Exp Cell Res 313: 4130-4144. (Pubitemid 350089966)
    • (2007) Experimental Cell Research , vol.313 , Issue.20 , pp. 4130-4144
    • De Leeuw, F.1    Zhang, T.2    Wauquier, C.3    Huez, G.4    Kruys, V.5    Gueydan, C.6
  • 11
    • 52949122554 scopus 로고    scopus 로고
    • TDRD3, a novel Tudor domain-containing protein, localizes to cytoplasmic stress granules
    • Goulet I, Boisvenue S, Mokas S, Mazroui R, Cote J. 2008. TDRD3, a novel Tudor domain-containing protein, localizes to cytoplasmic stress granules. Hum Mol Genet 17: 3055-3074.
    • (2008) Hum Mol Genet , vol.17 , pp. 3055-3074
    • Goulet, I.1    Boisvenue, S.2    Mokas, S.3    Mazroui, R.4    Cote, J.5
  • 12
    • 68949172267 scopus 로고    scopus 로고
    • Robust heat shock induces eIF2α-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, Vojtova J, Malinska K, Malcova I, Novakova L, Janoskova D, et al. 2009. Robust heat shock induces eIF2α-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    Vojtova, J.6    Malinska, K.7    Malcova, I.8    Novakova, L.9    Janoskova, D.10
  • 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
    • DOI 10.1083/jcb.200707010
    • 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. (Pubitemid 47606684)
    • (2007) Journal of Cell Biology , vol.179 , Issue.1 , pp. 65-74
    • Hoyle, N.P.1    Castelli, L.M.2    Campbell, S.G.3    Holmes, L.E.A.4    Ashe, M.P.5
  • 14
    • 4143097170 scopus 로고    scopus 로고
    • Survival motor neuron protein facilitates assembly of stress granules
    • DOI 10.1016/j.febslet.2004.07.010, PII S0014579304008671
    • Hua Y, Zhou J. 2004. Survival motor neuron protein facilitates assembly of stress granules. FEBS Lett 572: 69-74. (Pubitemid 39092515)
    • (2004) FEBS Letters , vol.572 , Issue.1-3 , pp. 69-74
    • Hua, Y.1    Zhou, J.2
  • 16
    • 38449123517 scopus 로고    scopus 로고
    • Mammalian stress granules and processing bodies
    • Kedersha N, Anderson P. 2007. Mammalian stress granules and processing bodies. Methods Enzymol 431: 61-81.
    • (2007) Methods Enzymol , vol.431 , pp. 61-81
    • Kedersha, N.1    Anderson, P.2
  • 17
    • 0033611157 scopus 로고    scopus 로고
    • RNA-binding proteins TIA-1 and TIAR link the phosphorylation of eIF-2α 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-2α 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
  • 19
    • 77957893483 scopus 로고    scopus 로고
    • A global census of fission yeast deubiquitinating enzyme localization and interaction networks reveals distinct compartmentalization profiles and overlapping functions in endocytosis and polarity
    • doi: 10.1371/journal.pbio.1000471
    • Kouranti I, McLean JR, Feoktistova A, Liang P, Johnson AE, Roberts-Galbraith RH, Gould KL. 2010. A global census of fission yeast deubiquitinating enzyme localization and interaction networks reveals distinct compartmentalization profiles and overlapping functions in endocytosis and polarity. PLoS Biol 8: e1000471. doi: 10.1371/journal.pbio.1000471.
    • (2010) PLoS Biol , vol.8
    • Kouranti, I.1    McLean, J.R.2    Feoktistova, A.3    Liang, P.4    Johnson, A.E.5    Roberts-Galbraith, R.H.6    Gould, K.L.7
  • 20
    • 55049098755 scopus 로고    scopus 로고
    • Heat shock causes a decrease in polysomes and the appearance of stress granules in trypanosomes independently of eIF2α phosphorylation at Thr169
    • Kramer S, Queiroz R, Ellis L, Webb H, Hoheisel JD, Clayton C, Carrington M. 2008. Heat shock causes a decrease in polysomes and the appearance of stress granules in trypanosomes independently of eIF2α phosphorylation at Thr169. J Cell Sci 121: 3002-3014.
    • (2008) J Cell Sci , vol.121 , pp. 3002-3014
    • Kramer, S.1    Queiroz, R.2    Ellis, L.3    Webb, H.4    Hoheisel, J.D.5    Clayton, C.6    Carrington, M.7
  • 21
    • 37449030154 scopus 로고    scopus 로고
    • The deacetylase HDAC6 is a novel critical component of stress granules involved in the stress response
    • Kwon S, Zhang Y, Matthias P. 2007. The deacetylase HDAC6 is a novel critical component of stress granules involved in the stress response. Genes Dev 21: 3381-3394.
    • (2007) Genes Dev , vol.21 , pp. 3381-3394
    • Kwon, S.1    Zhang, Y.2    Matthias, P.3
  • 22
  • 24
    • 0026025891 scopus 로고
    • Molecular genetic analysis of fission yeast Schizosaccharomyces pombe
    • Moreno S, Klar A, Nurse P. 1991. Molecular genetic analysis of fission yeast Schizosaccharomyces pombe. Methods Enzymol 194: 795-823.
    • (1991) Methods Enzymol , vol.194 , pp. 795-823
    • Moreno, S.1    Klar, A.2    Nurse, P.3
  • 25
    • 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
  • 27
    • 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
  • 29
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration
    • DOI 10.1038/13732
    • Rigaut G, Shevchenko A, Rutz B, Wilm M, Mann M, Seraphin B. 1999. A generic protein purification method for protein complex characterization and proteome exploration. Nat Biotechnol 17: 1030-1032. (Pubitemid 29474865)
    • (1999) Nature Biotechnology , vol.17 , Issue.10 , pp. 1030-1032
    • Rigaut, G.1    Shevchenko, A.2    Rutz, B.3    Wilm, M.4    Mann, M.5    Seraphin, B.6
  • 30
    • 0347504851 scopus 로고    scopus 로고
    • RNA-binding protein Csx1 mediates global control of gene expression in response to oxidative stress
    • DOI 10.1093/emboj/cdg597
    • Rodriguez-Gabriel MA, Burns G, McDonald WH, Martin V, Yates JR III, Bahler J, Russell P. 2003. RNA-binding protein Csx1 mediates global control of gene expression in response to oxidative stress. EMBO J 22: 6256-6266. (Pubitemid 37522583)
    • (2003) EMBO Journal , vol.22 , Issue.23 , pp. 6256-6266
    • Rodriguez-Gabriel, M.A.1    Burns, G.2    McDonald, W.H.3    Martin, V.4    Yates III, J.R.5    Bahler, J.6    Russell, P.7
  • 31
    • 1542782551 scopus 로고    scopus 로고
    • Cpc2/RACK1 is a ribosome-associated protein that promotes efficient translation in Schizosaccharomyces pombe
    • Shor B, Calaycay J, Rushbrook J, McLeod M. 2003. Cpc2/RACK1 is a ribosome-associated protein that promotes efficient translation in Schizosaccharomyces pombe. J Biol Chem 278: 49119-49128.
    • (2003) J Biol Chem , vol.278 , pp. 49119-49128
    • Shor, B.1    Calaycay, J.2    Rushbrook, J.3    McLeod, M.4
  • 32
    • 0026091180 scopus 로고
    • A polyadenylate binding protein localized to the granules of cytolytic lymphocytes induces DNA fragmentation in target cells
    • Tian Q, Streuli M, Saito H, Schlossman SF, Anderson P. 1991. A polyadenylate binding protein localized to the granules of cytolytic lymphocytes induces DNA fragmentation in target cells. Cell 67: 629-639. (Pubitemid 121001476)
    • (1991) Cell , vol.67 , Issue.3 , pp. 629-639
    • Tian, Q.1    Streuli, M.2    Saito, H.3    Schlossman, S.F.4    Anderson, P.5
  • 34
    • 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, Norbury CJ, Watt S, Bahler J, Wang SW. 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    Norbury, C.J.6    Watt, S.7    Bahler, J.8    Wang, S.W.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.