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Volumn 8, Issue 7, 2006, Pages 668-676

Activation of the DExD/H-box protein Dbp5 by the nuclear-pore protein Gle1 and its coactivator InsP6 is required for mRNA export

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; HOMEODOMAIN PROTEIN; INOSITOL POLYPHOSPHATE; MESSENGER RNA; NUCLEOPORIN; PHYTIC ACID; PROTEIN DBP5; PROTEIN GLE1; UNCLASSIFIED DRUG;

EID: 33745742173     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb1424     Document Type: Article
Times cited : (221)

References (43)
  • 1
    • 24644502657 scopus 로고    scopus 로고
    • From birth to death: The complex lives of eukaryotic mRNAs
    • Moore, M. J. From birth to death: The complex lives of eukaryotic mRNAs. Science 309, 1514-1518 (2005).
    • (2005) Science , vol.309 , pp. 1514-1518
    • Moore, M.J.1
  • 2
    • 1542344429 scopus 로고    scopus 로고
    • DEAD-box proteins: The driving forces behind RNA metabolism
    • Rocak, S. & Linder, P. DEAD-box proteins: The driving forces behind RNA metabolism. Nature Rev. Mol. Cell. Biol. 5, 232-241 (2004).
    • (2004) Nature Rev. Mol. Cell. Biol. , vol.5 , pp. 232-241
    • Rocak, S.1    Linder, P.2
  • 3
    • 0035808566 scopus 로고    scopus 로고
    • Active disruption of an RNA-protein interaction by a DExH/D RNA helicase
    • Jankowsky, E., Gross, C. H., Shuman, S. & Pyle, A. M. Active disruption of an RNA-protein interaction by a DExH/D RNA helicase. Science 291, 121-125 (2001).
    • (2001) Science , vol.291 , pp. 121-125
    • Jankowsky, E.1    Gross, C.H.2    Shuman, S.3    Pyle, A.M.4
  • 4
    • 2342443461 scopus 로고    scopus 로고
    • Protein displacement by DExH/D 'RNA helicases' without duplex unwinding
    • Fairman, M. E. et al. Protein displacement by DExH/D 'RNA helicases' without duplex unwinding. Science 304, 730-734 (2004).
    • (2004) Science , vol.304 , pp. 730-734
    • Fairman, M.E.1
  • 5
    • 0032079407 scopus 로고    scopus 로고
    • Dbp5p, a cytosolic RNA helicase, is required for poly(A)+ RNA export
    • Tseng, S. S. et al. Dbp5p, a cytosolic RNA helicase, is required for poly(A)+ RNA export. EMBO J. 17, 2651-2662 (1998).
    • (1998) EMBO J. , vol.17 , pp. 2651-2662
    • Tseng, S.S.1
  • 6
    • 0032080030 scopus 로고    scopus 로고
    • Dbp5p/Rat8p is a yeast nuclear pore-associated DEAD-box protein essential for RNA export
    • Snay-Hodge, C. A., Colot, H. V., Goldstein, A. L. & Cole, C. N. Dbp5p/ Rat8p is a yeast nuclear pore-associated DEAD-box protein essential for RNA export. EMBO J. 17, 2663-2676 (1998).
    • (1998) EMBO J. , vol.17 , pp. 2663-2676
    • Snay-Hodge, C.A.1    Colot, H.V.2    Goldstein, A.L.3    Cole, C.N.4
  • 7
    • 0033517108 scopus 로고    scopus 로고
    • Dbp5, a DEAD-box protein required for mRNA export, is recruited to the cytoplasmic fibrils of nuclear pore complex via a conserved interaction with CAN/Nup159p
    • Schmitt, C. et al. Dbp5, a DEAD-box protein required for mRNA export, is recruited to the cytoplasmic fibrils of nuclear pore complex via a conserved interaction with CAN/Nup159p. EMBO J. 18, 4332-4347 (1999).
    • (1999) EMBO J. , vol.18 , pp. 4332-4347
    • Schmitt, C.1
  • 8
    • 0033569962 scopus 로고    scopus 로고
    • Rat8p/Dbp5p is a shuttling transport factor that interacts with Rat7p/Nup159p and Gle1p and suppresses the mRNA export defect of xpo1-1 cells
    • Hodge, C. A., Colot, H. V., Stafford, P. & Cole, C. N. Rat8p/Dbp5p is a shuttling transport factor that interacts with Rat7p/Nup159p and Gle1p and suppresses the mRNA export defect of xpo1-1 cells. EMBO J. 18, 5778-5788 (1999).
    • (1999) EMBO J. , vol.18 , pp. 5778-5788
    • Hodge, C.A.1    Colot, H.V.2    Stafford, P.3    Cole, C.N.4
  • 9
    • 0033569797 scopus 로고    scopus 로고
    • The RNA export factor Gle1p is located on the cytoplasmic fibrils of the NPC and physically interacts with the FG-nucleoporin Rip1p, the DEAD-box protein Rat8p/Dbp5p and a new protein Ymr 255p
    • Strahm, Y. et al. The RNA export factor Gle1p is located on the cytoplasmic fibrils of the NPC and physically interacts with the FG-nucleoporin Rip1p, the DEAD-box protein Rat8p/Dbp5p and a new protein Ymr 255p. EMBO J. 18, 5761-5777 (1999).
    • (1999) EMBO J. , vol.18 , pp. 5761-5777
    • Strahm, Y.1
  • 10
    • 9744266768 scopus 로고    scopus 로고
    • The N-terminal domain of Nup159 forms a beta-propeller that functions in mRNA export by tethering the helicase Dbp5 to the nuclear pore
    • Weirich, C. S., Erzberger, J. P., Berger, J. M. & Weis, K. The N-terminal domain of Nup159 forms a beta-propeller that functions in mRNA export by tethering the helicase Dbp5 to the nuclear pore. Mol. Cell 16, 749-760 (2004).
    • (2004) Mol. Cell , vol.16 , pp. 749-760
    • Weirich, C.S.1    Erzberger, J.P.2    Berger, J.M.3    Weis, K.4
  • 11
    • 0030827396 scopus 로고    scopus 로고
    • The yeast nucleoporin rip1p contributes to multiple export pathways with no essential role for its FG-repeat region
    • Stutz, F. et al. The yeast nucleoporin rip1p contributes to multiple export pathways with no essential role for its FG-repeat region. Genes Dev. 11, 2857-2868 (1997).
    • (1997) Genes Dev. , vol.11 , pp. 2857-2868
    • Stutz, F.1
  • 12
    • 9844219734 scopus 로고    scopus 로고
    • Yeast heat shock mRNAs are exported through a distinct pathway defined by Rip1p
    • Saavedra, C. A., Hammell, C. M., Heath, C. V. & Cole, C. N. Yeast heat shock mRNAs are exported through a distinct pathway defined by Rip1p. Genes Dev. 11, 2845-2856 (1997).
    • (1997) Genes Dev. , vol.11 , pp. 2845-2856
    • Saavedra, C.A.1    Hammell, C.M.2    Heath, C.V.3    Cole, C.N.4
  • 13
    • 27944474017 scopus 로고    scopus 로고
    • The DEAD-box protein Dbp5p is required to dissociate Mex67p from exported mRNPs at the nuclear rim
    • Lund, M. K. & Guthrie, C. The DEAD-box protein Dbp5p is required to dissociate Mex67p from exported mRNPs at the nuclear rim. Mol. Cell 20, 645-651 (2005).
    • (2005) Mol. Cell , vol.20 , pp. 645-651
    • Lund, M.K.1    Guthrie, C.2
  • 14
    • 0036500482 scopus 로고    scopus 로고
    • The mRNA export factor Dbp5 is associated with Balbiani ring mRNP from gene to cytoplasm
    • Zhao, J., Jin, S. B., Bjorkroth, B., Wieslander, L. & Daneholt, B. The mRNA export factor Dbp5 is associated with Balbiani ring mRNP from gene to cytoplasm. EMBO J. 21, 1177-1187 (2002).
    • (2002) EMBO J. , vol.21 , pp. 1177-1187
    • Zhao, J.1    Jin, S.B.2    Bjorkroth, B.3    Wieslander, L.4    Daneholt, B.5
  • 15
    • 0037884974 scopus 로고    scopus 로고
    • An early function during transcription for the yeast mRNA export factor Dbp5p/Rat8p suggested by its genetic and physical interactions with transcription factor IIH components
    • Estruch, F. & Cole, C. N. An early function during transcription for the yeast mRNA export factor Dbp5p/Rat8p suggested by its genetic and physical interactions with transcription factor IIH components. Mol. Biol. Cell 14, 1664-1676 (2003).
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1664-1676
    • Estruch, F.1    Cole, C.N.2
  • 16
    • 0033516604 scopus 로고    scopus 로고
    • A phospholipase C-dependent inositol polyphosphate kinase pathway required for efficient messenger RNA export
    • York, J. D., Odom, A. R., Murphy, R., Ives, E. B. & Wente, S. R. A phospholipase C-dependent inositol polyphosphate kinase pathway required for efficient messenger RNA export. Science 285, 96-100 (1999).
    • (1999) Science , vol.285 , pp. 96-100
    • York, J.D.1    Odom, A.R.2    Murphy, R.3    Ives, E.B.4    Wente, S.R.5
  • 17
    • 10944261830 scopus 로고    scopus 로고
    • Cytoplasmic inositol hexakisphosphate production is sufficient for mediating the Gle1-mRNA export pathway
    • Miller, A. L. et al. Cytoplasmic inositol hexakisphosphate production is sufficient for mediating the Gle1-mRNA export pathway. J. Biol. Chem. 279, 51022-51032 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 51022-51032
    • Miller, A.L.1
  • 18
    • 0037090684 scopus 로고    scopus 로고
    • Specific interaction of IP6 with human Ku70/80, the DNA-binding subunit of DNA-PK
    • Hanakahi, L. A. & West, S. C. Specific interaction of IP6 with human Ku70/80, the DNA-binding subunit of DNA-PK. EMBO J. 21, 2038-2044 (2002).
    • (2002) EMBO J. , vol.21 , pp. 2038-2044
    • Hanakahi, L.A.1    West, S.C.2
  • 19
    • 0037192767 scopus 로고    scopus 로고
    • Binding of inositol hexakisphosphate (IP6) to Ku but not to DNA-PKcs
    • Ma, Y. & Lieber, M. R. Binding of inositol hexakisphosphate (IP6) to Ku but not to DNA-PKcs. J. Biol. Chem. 277, 10756-10759 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 10756-10759
    • Ma, Y.1    Lieber, M.R.2
  • 20
    • 0034664805 scopus 로고    scopus 로고
    • Binding of inositol phosphate to DNA-PK and stimulation of double-strand break repair
    • Hanakahi, L. A., Bartlet-Jones, M., Chappell, C., Pappin, D. & West, S. C. Binding of inositol phosphate to DNA-PK and stimulation of double-strand break repair. Cell 102, 721-729 (2000).
    • (2000) Cell , vol.102 , pp. 721-729
    • Hanakahi, L.A.1    Bartlet-Jones, M.2    Chappell, C.3    Pappin, D.4    West, S.C.5
  • 21
    • 0037414839 scopus 로고    scopus 로고
    • Modulation of ATP-dependent chromatin-remodeling complexes by inositol polyphosphates
    • Shen, X., Xiao, H., Ranallo, R., Wu, W. H. & Wu, C. Modulation of ATP-dependent chromatin-remodeling complexes by inositol polyphosphates. Science 299, 112-114 (2003).
    • (2003) Science , vol.299 , pp. 112-114
    • Shen, X.1    Xiao, H.2    Ranallo, R.3    Wu, W.H.4    Wu, C.5
  • 22
    • 0037414868 scopus 로고    scopus 로고
    • Regulation of chromatin remodeling by inositol polyphosphates
    • Steger, D. J., Haswell, E. S., Miller, A. L., Wente, S. R. & O'Shea, E. K. Regulation of chromatin remodeling by inositol polyphosphates. Science 299, 114-116 (2003).
    • (2003) Science , vol.299 , pp. 114-116
    • Steger, D.J.1    Haswell, E.S.2    Miller, A.L.3    Wente, S.R.4    O'Shea, E.K.5
  • 23
    • 13844311012 scopus 로고    scopus 로고
    • Inositol pyrophosphates regulate cell death and telomere length through phosphoinositide 3-kinase-related protein kinases
    • Saiardi, A., Resnick, A. C., Snowman, A. M., Wendland, B. & Snyder, S. H. Inositol pyrophosphates regulate cell death and telomere length through phosphoinositide 3-kinase-related protein kinases. Proc. Natl Acad. Sci. USA 102, 1911-1914 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 1911-1914
    • Saiardi, A.1    Resnick, A.C.2    Snowman, A.M.3    Wendland, B.4    Snyder, S.H.5
  • 26
    • 24644519954 scopus 로고    scopus 로고
    • Inositol hexakisphosphate is bound in the ADAR2 core and required for RNA editing
    • Macbeth, M. R. et al. Inositol hexakisphosphate is bound in the ADAR2 core and required for RNA editing. Science 309, 1534-1539 (2005).
    • (2005) Science , vol.309 , pp. 1534-1539
    • Macbeth, M.R.1
  • 27
    • 0027304451 scopus 로고
    • Genetic and biochemical characterization of a phosphatidylinositol-specific phospholipase C in Saccharomyces cerevisiae
    • Flick, J. S. & Thorner, J. Genetic and biochemical characterization of a phosphatidylinositol-specific phospholipase C in Saccharomyces cerevisiae. Mol. Cell. Biol. 13, 5861-5876 (1993).
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5861-5876
    • Flick, J.S.1    Thorner, J.2
  • 28
    • 0034677903 scopus 로고    scopus 로고
    • A role for nuclear inositol 1,4,5-trisphosphate kinase in transcriptional control
    • Odom, A. R., Stahlberg, A., Wente, S. R. & York, J. D. A role for nuclear inositol 1,4,5-trisphosphate kinase in transcriptional control. Science 287, 2026-2029 (2000).
    • (2000) Science , vol.287 , pp. 2026-2029
    • Odom, A.R.1    Stahlberg, A.2    Wente, S.R.3    York, J.D.4
  • 29
    • 0033581832 scopus 로고    scopus 로고
    • Synthesis of diphosphoinositol pentakisphosphate by a newly identified family of higher inositol polyphosphate kinases
    • Saiardi, A., Erdjument-Bromage, H., Snowman, A. M., Tempst, P. & Snyder, S. H. Synthesis of diphosphoinositol pentakisphosphate by a newly identified family of higher inositol polyphosphate kinases. Curr. Biol. 9, 1323-1326 (1999).
    • (1999) Curr. Biol. , vol.9 , pp. 1323-1326
    • Saiardi, A.1    Erdjument-Bromage, H.2    Snowman, A.M.3    Tempst, P.4    Snyder, S.H.5
  • 30
    • 33344473656 scopus 로고    scopus 로고
    • The DEAD-box protein family of RNA helicases
    • Cordin, O., Banroques, J., Tanner, N. K. & Linder, P. The DEAD-box protein family of RNA helicases. Gene 367, 17-37 (2006).
    • (2006) Gene , vol.367 , pp. 17-37
    • Cordin, O.1    Banroques, J.2    Tanner, N.K.3    Linder, P.4
  • 31
    • 0030722640 scopus 로고    scopus 로고
    • Glycolytic flux is conditionally correlated with ATP concentration in Saccharomyces cerevisiae: A chemostat study under carbon- or nitrogen-limiting conditions
    • Larsson, C., Nilsson, A., Blomberg, A. & Gustafsson, L. Glycolytic flux is conditionally correlated with ATP concentration in Saccharomyces cerevisiae: A chemostat study under carbon- or nitrogen-limiting conditions. J. Bacteriol. 179, 7243-7250 (1997).
    • (1997) J. Bacteriol. , vol.179 , pp. 7243-7250
    • Larsson, C.1    Nilsson, A.2    Blomberg, A.3    Gustafsson, L.4
  • 32
    • 15744369249 scopus 로고    scopus 로고
    • Physical and genetic interactions link the yeast protein Zds1p with mRNA nuclear export
    • Estruch, F., Hodge, C. A., Rodriguez-Navarro, S. & Cole, C. N. Physical and genetic interactions link the yeast protein Zds1p with mRNA nuclear export. J. Biol. Chem. 280, 9691-9697 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 9691-9697
    • Estruch, F.1    Hodge, C.A.2    Rodriguez-Navarro, S.3    Cole, C.N.4
  • 34
    • 27144445082 scopus 로고    scopus 로고
    • The exon junction core complex is locked onto RNA by inhibition of eIF4AIII ATPase activity
    • Ballut, L. et al. The exon junction core complex is locked onto RNA by inhibition of eIF4AIII ATPase activity. Nature Struct. Mol. Biol. 12, 861-869 (2005).
    • (2005) Nature Struct. Mol. Biol. , vol.12 , pp. 861-869
    • Ballut, L.1
  • 35
    • 2442694192 scopus 로고    scopus 로고
    • The nuclear pore complex and the DEAD box protein Rat8p/Dbp5p have nonessential features which appear to facilitate mRNA export following heat shock
    • Rollenhagen, C., Hodge, C. A. & Cole, C. N. The nuclear pore complex and the DEAD box protein Rat8p/Dbp5p have nonessential features which appear to facilitate mRNA export following heat shock. Mol. Cell. Biol. 24, 4869-4879 (2004).
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4869-4879
    • Rollenhagen, C.1    Hodge, C.A.2    Cole, C.N.3
  • 36
    • 4944234419 scopus 로고    scopus 로고
    • Stress response in yeast mRNA export factor: Reversible changes in Rat8p localization are caused by ethanol stress but not heat shock
    • Takemura, R., Inoue, Y. & Izawa, S. Stress response in yeast mRNA export factor: Reversible changes in Rat8p localization are caused by ethanol stress but not heat shock. J. Cell Sci. 117, 4189-4197 (2004).
    • (2004) J. Cell Sci. , vol.117 , pp. 4189-4197
    • Takemura, R.1    Inoue, Y.2    Izawa, S.3
  • 37
    • 0034107101 scopus 로고    scopus 로고
    • Nuclear export of heat shock and non-heatshock mRNA occurs via similar pathways
    • Vainberg, I. E., Dower, K. & Rosbash, M. Nuclear export of heat shock and non-heatshock mRNA occurs via similar pathways. Mol. Cell. Biol. 20, 3996-4005 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3996-4005
    • Vainberg, I.E.1    Dower, K.2    Rosbash, M.3
  • 39
    • 0030979410 scopus 로고    scopus 로고
    • Structure of the hepatitis C virus RNA helicase domain
    • Yao, N. et al. Structure of the hepatitis C virus RNA helicase domain. Nature Struct. Biol. 4, 463-467 (1997).
    • (1997) Nature Struct. Biol. , vol.4 , pp. 463-467
    • Yao, N.1
  • 40
    • 26644450709 scopus 로고    scopus 로고
    • ATP- and ADP-Dependent modulation of RNA unwinding and strand annealing activities by the DEAD-box protein DED1
    • Yang, Q. & Jankowsky, E. ATP- and ADP-Dependent modulation of RNA unwinding and strand annealing activities by the DEAD-box protein DED1. Biochemistry 44, 13591-13601 (2005).
    • (2005) Biochemistry , vol.44 , pp. 13591-13601
    • Yang, Q.1    Jankowsky, E.2
  • 41
    • 0028363764 scopus 로고
    • Drosophila kinesin minimal motor domain expressed in Escherichia coli. Purification and kinetic characterization
    • Huang, T. G. & Hackney, D. D. Drosophila kinesin minimal motor domain expressed in Escherichia coli. Purification and kinetic characterization. J. Biol. Chem. 269, 16493-16501 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 16493-16501
    • Huang, T.G.1    Hackney, D.D.2
  • 42
    • 0020645052 scopus 로고
    • Yeast promoters and lacZ fusions designed to study expression of cloned genes in yeast
    • Guarente, L. Yeast promoters and lacZ fusions designed to study expression of cloned genes in yeast. Methods Enzymol 101, 181-191 (1983).
    • (1983) Methods Enzymol , vol.101 , pp. 181-191
    • Guarente, L.1
  • 43
    • 0035164676 scopus 로고    scopus 로고
    • The nuclear export receptor Xpo1p forms distinct complexes with NES transport substrates and the yeast Ran binding protein 1 (Yrb1p)
    • Maurer, P. et al. The nuclear export receptor Xpo1p forms distinct complexes with NES transport substrates and the yeast Ran binding protein 1 (Yrb1p). Mol. Biol. Cell 12, 539-549 (2001).
    • (2001) Mol. Biol. Cell , vol.12 , pp. 539-549
    • Maurer, P.1


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