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Volumn 179, Issue 1, 2007, Pages 65-74

Stress-dependent relocalization of translationally primed mRNPs to cytoplasmic granules that are kinetically and spatially distinct from P-bodies

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; RNA;

EID: 35348989809     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.200707010     Document Type: Article
Times cited : (194)

References (39)
  • 1
    • 0031041015 scopus 로고    scopus 로고
    • A novel inhibitor of cap-dependent translation initiation in yeast: P20 competes with eIF4G for binding to eIF4E
    • Altmann, M., N. Schmitz, C. Berset, and H. Trachsel. 1997. A novel inhibitor of cap-dependent translation initiation in yeast: p20 competes with eIF4G for binding to eIF4E. EMBO J. 16:1114-1121.
    • (1997) EMBO J , vol.16 , pp. 1114-1121
    • Altmann, M.1    Schmitz, N.2    Berset, C.3    Trachsel, H.4
  • 3
    • 17844371700 scopus 로고    scopus 로고
    • A role for eIF4E and eIF4E-transporter in targeting mRNPs to mammalian processing bodies
    • Andrei, M.A., D. Ingelfinger, R. Heintzmann, T. Achsel, R. Rivera-Pomar, and R. Luhrmann. 2005. A role for eIF4E and eIF4E-transporter in targeting mRNPs to mammalian processing bodies. RNA. 11:717-727.
    • (2005) RNA , vol.11 , pp. 717-727
    • Andrei, M.A.1    Ingelfinger, D.2    Heintzmann, R.3    Achsel, T.4    Rivera-Pomar, R.5    Luhrmann, R.6
  • 4
    • 0034100041 scopus 로고    scopus 로고
    • Glucose depletion rapidly inhibits translation initiation in yeast
    • Ashe, M.P., S.K. De Long, and A.B. Sachs. 2000. Glucose depletion rapidly inhibits translation initiation in yeast. Mol. Biol. Cell. 11:833-848.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 833-848
    • Ashe, M.P.1    De Long, S.K.2    Sachs, A.B.3
  • 5
    • 0035890059 scopus 로고    scopus 로고
    • A novel eIF2B-dependent mechanism of translational control in yeast as a response to fusel alcohols
    • Ashe, M.P., J.W. Slaven, S.K. De Long, S. Ibrahimo, and A.B. Sachs. 2001. A novel eIF2B-dependent mechanism of translational control in yeast as a response to fusel alcohols. EMBO J. 20:6464-6474.
    • (2001) EMBO J , vol.20 , pp. 6464-6474
    • Ashe, M.P.1    Slaven, J.W.2    De Long, S.K.3    Ibrahimo, S.4    Sachs, A.B.5
  • 6
    • 34347387606 scopus 로고    scopus 로고
    • Accumulation of polyadenylated mRNA, Pab1p, eIF4E, and eIF4G with P-bodies in Saccharomyces cerevisiae
    • Brengues, M., and R. Parker. 2007. Accumulation of polyadenylated mRNA, Pab1p, eIF4E, and eIF4G with P-bodies in Saccharomyces cerevisiae. Mol. Biol. Cell. 18:2592-2602.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 2592-2602
    • Brengues, M.1    Parker, R.2
  • 7
    • 27144515901 scopus 로고    scopus 로고
    • Movement of eukaryotic mRNAs between polysomes and cytoplasmic processing bodies
    • Brengues, M., D. Teixeira, and R. Parker. 2005. Movement of eukaryotic mRNAs between polysomes and cytoplasmic processing bodies. Science. 310:486-489.
    • (2005) Science , vol.310 , pp. 486-489
    • Brengues, M.1    Teixeira, D.2    Parker, R.3
  • 8
    • 0034544815 scopus 로고    scopus 로고
    • Pre-mRNA processing factors are required for nuclear export
    • Brodsky, A.S., and P.A. Silver. 2000. Pre-mRNA processing factors are required for nuclear export. RNA. 6:1737-1749.
    • (2000) RNA , vol.6 , pp. 1737-1749
    • Brodsky, A.S.1    Silver, P.A.2
  • 10
    • 24944495906 scopus 로고    scopus 로고
    • Dynamic cycling of eIF2 through a large eIF2B-containing cytoplasmic body: Implications for translation control
    • Campbell, S.G., N.P. Hoyle, and M.P. Ashe. 2005. Dynamic cycling of eIF2 through a large eIF2B-containing cytoplasmic body: implications for translation control. J. Cell Biol. 170:925-934.
    • (2005) J. Cell Biol , vol.170 , pp. 925-934
    • Campbell, S.G.1    Hoyle, N.P.2    Ashe, M.P.3
  • 11
    • 18844397041 scopus 로고    scopus 로고
    • A new paradigm for translational control: Inhibition via 5′-3′ mRNA tethering by Bicoid and the eIF4E cognate 4EHP
    • Cho, P.F., F. Poulin, Y.A. Cho-Park, I.B. Cho-Park, J.D. Chicoine, P. Lasko, and N. Sonenberg. 2005. A new paradigm for translational control: inhibition via 5′-3′ mRNA tethering by Bicoid and the eIF4E cognate 4EHP. Cell. 121:411-423.
    • (2005) Cell , vol.121 , pp. 411-423
    • Cho, P.F.1    Poulin, F.2    Cho-Park, Y.A.3    Cho-Park, I.B.4    Chicoine, J.D.5    Lasko, P.6    Sonenberg, N.7
  • 12
    • 2442566370 scopus 로고    scopus 로고
    • Cytoplasmic foci are sites of mRNA decay in human cells
    • Cougot, N., S. Babajko, and B. Seraphin. 2004. Cytoplasmic foci are sites of mRNA decay in human cells. J. Cell Biol. 165:31-40.
    • (2004) J. Cell Biol , vol.165 , pp. 31-40
    • Cougot, N.1    Babajko, S.2    Seraphin, B.3
  • 14
    • 0028059555 scopus 로고
    • Iron regulatory protein prevents binding of the 43S translation pre-initiation complex to ferritin and eALAS mRNAs
    • Gray, N.K., and M.W. Hentze. 1994. Iron regulatory protein prevents binding of the 43S translation pre-initiation complex to ferritin and eALAS mRNAs. EMBO J. 13:3882-3891.
    • (1994) EMBO J , vol.13 , pp. 3882-3891
    • Gray, N.K.1    Hentze, M.W.2
  • 15
    • 27144510561 scopus 로고    scopus 로고
    • Translational regulation of GCN4 and the general amino acid control of yeast
    • Hinnebusch, A.G. 2005. Translational regulation of GCN4 and the general amino acid control of yeast. Annu. Rev. Microbiol. 59:407-450.
    • (2005) Annu. Rev. Microbiol , vol.59 , pp. 407-450
    • Hinnebusch, A.G.1
  • 16
    • 1642363230 scopus 로고    scopus 로고
    • Loss of translational control in yeast compromised for the major mRNA decay pathway
    • Holmes, L.E., S.G. Campbell, S.K. De Long, A.B. Sachs, and M.P. Ashe. 2004. Loss of translational control in yeast compromised for the major mRNA decay pathway. Mol. Cell. Biol. 24:2998-3010.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 2998-3010
    • Holmes, L.E.1    Campbell, S.G.2    De Long, S.K.3    Sachs, A.B.4    Ashe, M.P.5
  • 17
    • 33751571405 scopus 로고    scopus 로고
    • Regulation of translation initiation by the yeast eIF4E binding proteins is required for the pseudohyphal response
    • Ibrahimo, S., L.E. Holmes, and M.P. Ashe. 2006. Regulation of translation initiation by the yeast eIF4E binding proteins is required for the pseudohyphal response. Yeast. 23:1075-1088.
    • (2006) Yeast , vol.23 , pp. 1075-1088
    • Ibrahimo, S.1    Holmes, L.E.2    Ashe, M.P.3
  • 19
    • 33846004827 scopus 로고    scopus 로고
    • L13a blocks 48S assembly: Role of a general initiation factor in mRNA-specific translational control
    • Kapasi, P., S. Chaudhuri, K. Vyas, D. Baus, A.A. Komar, P.L. Fox, W.C. Merrick, and B. Mazumder. 2007. L13a blocks 48S assembly: role of a general initiation factor in mRNA-specific translational control. Mol. Cell. 25:113-126.
    • (2007) Mol. Cell , vol.25 , pp. 113-126
    • Kapasi, P.1    Chaudhuri, S.2    Vyas, K.3    Baus, D.4    Komar, A.A.5    Fox, P.L.6    Merrick, W.C.7    Mazumder, B.8
  • 20
    • 3943080710 scopus 로고    scopus 로고
    • The molecular mechanics of eukaryotic translation
    • Kapp, L.D., and J.R. Lorsch. 2004. The molecular mechanics of eukaryotic translation. Annu. Rev. Biochem. 73:657-704.
    • (2004) Annu. Rev. Biochem , vol.73 , pp. 657-704
    • Kapp, L.D.1    Lorsch, J.R.2
  • 21
    • 0036863320 scopus 로고    scopus 로고
    • Stress granules: Sites of mRNA triage that regulate mRNA stability and translatability
    • Kedersha, N., and P. Anderson. 2002. Stress granules: sites of mRNA triage that regulate mRNA stability and translatability. Biochem. Soc. Trans. 30:963-969.
    • (2002) Biochem. Soc. Trans , vol.30 , pp. 963-969
    • Kedersha, N.1    Anderson, P.2
  • 22
    • 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, N.L., M. Gupta, W. Li, I. Miller, and P. Anderson. 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
  • 25
    • 0035213589 scopus 로고    scopus 로고
    • Assembly of the Drosophila germ plasm
    • Mahowald, A.P. 2001. Assembly of the Drosophila germ plasm. Int. Rev. Cytol. 203:187-213.
    • (2001) Int. Rev. Cytol , vol.203 , pp. 187-213
    • Mahowald, A.P.1
  • 26
    • 0032160381 scopus 로고    scopus 로고
    • IRP-1 binding to ferritin mRNA prevents the recruitment of the small ribosomal subunit by the cap-binding complex eIF4F
    • Muckenthaler, M., N.K. Gray, and M.W. Hentze. 1998. IRP-1 binding to ferritin mRNA prevents the recruitment of the small ribosomal subunit by the cap-binding complex eIF4F. Mol. Cell. 2:383-388.
    • (1998) Mol. Cell , vol.2 , pp. 383-388
    • Muckenthaler, M.1    Gray, N.K.2    Hentze, M.W.3
  • 27
    • 0034973590 scopus 로고    scopus 로고
    • Transcriptional profi ling shows that Gcn4p is a master regulator of gene expression during amino acid starvation in yeast
    • Natarajan, K., M.R. Meyer, B.M. Jackson, D. Slade, C. Roberts, A.G. Hinnebusch, and M.J. Marton. 2001. Transcriptional profi ling shows that Gcn4p is a master regulator of gene expression during amino acid starvation in yeast. Mol. Cell. Biol. 21:4347-4368.
    • (2001) Mol. Cell. Biol , vol.21 , pp. 4347-4368
    • Natarajan, K.1    Meyer, M.R.2    Jackson, B.M.3    Slade, D.4    Roberts, C.5    Hinnebusch, A.G.6    Marton, M.J.7
  • 28
    • 0032777549 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factors 4G and 4A from Saccharomyces cerevisiae interact physically and functionally
    • Neff, C.L., and A.B. Sachs. 1999. Eukaryotic translation initiation factors 4G and 4A from Saccharomyces cerevisiae interact physically and functionally. Mol. Cell. Biol. 19:5557-5564.
    • (1999) Mol. Cell. Biol , vol.19 , pp. 5557-5564
    • Neff, C.L.1    Sachs, A.B.2
  • 29
    • 1842576663 scopus 로고    scopus 로고
    • Functions of eIF3 downstream of 48S assembly impact AUG recognition and GCN4 translational control
    • Nielsen, K.H., B. Szamecz, L. Valasek, A. Jivotovskaya, B.S. Shin, and A.G. Hinnebusch. 2004. Functions of eIF3 downstream of 48S assembly impact AUG recognition and GCN4 translational control. EMBO J. 23:1166-1177.
    • (2004) EMBO J , vol.23 , pp. 1166-1177
    • Nielsen, K.H.1    Szamecz, B.2    Valasek, L.3    Jivotovskaya, A.4    Shin, B.S.5    Hinnebusch, A.G.6
  • 30
    • 33847417585 scopus 로고    scopus 로고
    • P bodies and the control of mRNA translation and degradation
    • Parker, R., and U. Sheth. 2007. P bodies and the control of mRNA translation and degradation. Mol. Cell. 25:635-646.
    • (2007) Mol. Cell , vol.25 , pp. 635-646
    • Parker, R.1    Sheth, U.2
  • 31
    • 13444259647 scopus 로고    scopus 로고
    • Regulation of cap-dependent translation by eIF4E inhibitory proteins
    • Richter, J.D., and N. Sonenberg. 2005. Regulation of cap-dependent translation by eIF4E inhibitory proteins. Nature. 433:477-480.
    • (2005) Nature , vol.433 , pp. 477-480
    • Richter, J.D.1    Sonenberg, N.2
  • 32
    • 0002411516 scopus 로고    scopus 로고
    • Physical and functional interactions between the mRNA cap structure and the poly(A) tail
    • N. Sonenberg, J.W.B. Hershey, and M.B. Matthews, editors. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
    • Sachs, A.B. 2000. Physical and functional interactions between the mRNA cap structure and the poly(A) tail. In Translational Control of Gene Expression. N. Sonenberg, J.W.B. Hershey, and M.B. Matthews, editors. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY. 447-465.
    • (2000) Translational Control of Gene Expression , pp. 447-465
    • Sachs, A.B.1
  • 33
    • 0002791155 scopus 로고    scopus 로고
    • Interaction of mRNA translation and mRNA degradation in Saccharomyces cerevisiae
    • N. Sonenberg, J.W.B. Hershey, and M.B. Matthews, editors. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
    • Schwartz, D.C., and R. Parker. 2000. Interaction of mRNA translation and mRNA degradation in Saccharomyces cerevisiae. In Translational Control of Gene Expression. N. Sonenberg, J.W.B. Hershey, and M.B. Matthews, editors. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY. 807-826.
    • (2000) Translational Control of Gene Expression , pp. 807-826
    • Schwartz, D.C.1    Parker, R.2
  • 34
    • 0037968357 scopus 로고    scopus 로고
    • Decapping and decay of messenger RNA occur in cytoplasmic processing bodies
    • Sheth, U., and R. Parker. 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
  • 35
    • 33744977432 scopus 로고    scopus 로고
    • Targeting of aberrant mRNAs to cytoplasmic processing bodies
    • Sheth, U., and R. Parker. 2006. Targeting of aberrant mRNAs to cytoplasmic processing bodies. Cell. 125:1095-1109.
    • (2006) Cell , vol.125 , pp. 1095-1109
    • Sheth, U.1    Parker, R.2
  • 36
    • 27144465421 scopus 로고    scopus 로고
    • Global gene expression profi ling reveals widespread yet distinctive translational responses to different eukaryotic translation initiation factor 2B-targeting stress pathways
    • Smirnova, J.B., J.N. Selley, F. Sanchez-Cabo, K. Carroll, A.A. Eddy, J.E. McCarthy, S.J. Hubbard, G.D. Pavitt, C.M. Grant, and M.P. Ashe. 2005. Global gene expression profi ling reveals widespread yet distinctive translational responses to different eukaryotic translation initiation factor 2B-targeting stress pathways. Mol. Cell. Biol. 25:9340-9349.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 9340-9349
    • Smirnova, J.B.1    Selley, J.N.2    Sanchez-Cabo, F.3    Carroll, K.4    Eddy, A.A.5    McCarthy, J.E.6    Hubbard, S.J.7    Pavitt, G.D.8    Grant, C.M.9    Ashe, M.P.10
  • 37
    • 0009656730 scopus 로고
    • Immunofl uorescence visualization of germline-specific cytoplasmic granules in embryos, larvae, and adults of Caenorhabditis elegans
    • Strome, S., and W.B. Wood. 1982. Immunofl uorescence visualization of germline-specific cytoplasmic granules in embryos, larvae, and adults of Caenorhabditis elegans. Proc. Natl. Acad. Sci. USA. 79:1558-1562.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 1558-1562
    • Strome, S.1    Wood, W.B.2
  • 38
    • 15444379718 scopus 로고    scopus 로고
    • Processing bodies require RNA for assembly and contain nontranslating mRNAs
    • Teixeira, D., U. Sheth, M.A. Valencia-Sanchez, M. Brengues, and R. Parker. 2005. Processing bodies require RNA for assembly and contain nontranslating mRNAs. RNA. 11:371-382.
    • (2005) RNA , vol.11 , pp. 371-382
    • Teixeira, D.1    Sheth, U.2    Valencia-Sanchez, M.A.3    Brengues, M.4    Parker, R.5
  • 39
    • 0036428702 scopus 로고    scopus 로고
    • Intracellular translation initiation factor levels in Saccharomyces cerevisiae and their role in cap-complex function
    • von der Haar, T., and J.E. McCarthy. 2002. Intracellular translation initiation factor levels in Saccharomyces cerevisiae and their role in cap-complex function. Mol. Microbiol. 46:531-544.
    • (2002) Mol. Microbiol , vol.46 , pp. 531-544
    • von der Haar, T.1    McCarthy, J.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.