메뉴 건너뛰기




Volumn 18, Issue 3, 2006, Pages 299-306

Transport of messenger RNA from the nucleus to the cytoplasm

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; DEAD BOX PROTEIN; KARYOPHERIN; MESSENGER RNA; NUCLEOPORIN; PHOSPHATIDYLINOSITIDE; PROTEIN DBP5; PROTEIN GLE1; PROTEIN NUP159; RIBONUCLEOPROTEIN; UNCLASSIFIED DRUG;

EID: 33646516400     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2006.04.006     Document Type: Review
Times cited : (105)

References (57)
  • 1
    • 19344363274 scopus 로고    scopus 로고
    • Cotranscriptional mRNP assembly: from the DNA to the nuclear pore
    • Aguilera A. Cotranscriptional mRNP assembly: from the DNA to the nuclear pore. Curr Opin Cell Biol 17 (2005) 242-250
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 242-250
    • Aguilera, A.1
  • 2
    • 19344378943 scopus 로고    scopus 로고
    • Rules of engagement: co-transcriptional recruitment of pre-mRNA processing factors
    • Bentley D.L. Rules of engagement: co-transcriptional recruitment of pre-mRNA processing factors. Curr Opin Cell Biol 17 (2005) 251-256
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 251-256
    • Bentley, D.L.1
  • 3
    • 19344374094 scopus 로고    scopus 로고
    • TREX, SR proteins and export of mRNA
    • Reed R., and Cheng H. TREX, SR proteins and export of mRNA. Curr Opin Cell Biol 17 (2005) 269-273
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 269-273
    • Reed, R.1    Cheng, H.2
  • 6
    • 0024973850 scopus 로고
    • Some cis- and trans-acting mutants for splicing target pre-mRNA to the cytoplasm
    • Legrain P., and Rosbash M. Some cis- and trans-acting mutants for splicing target pre-mRNA to the cytoplasm. Cell 57 (1989) 573-583
    • (1989) Cell , vol.57 , pp. 573-583
    • Legrain, P.1    Rosbash, M.2
  • 7
    • 15444366645 scopus 로고    scopus 로고
    • Yeast poly(A)-binding protein Pab1 shuttles between the nucleus and the cytoplasm and functions in mRNA export
    • Brune C., Munchel S.E., Fischer N., Podtelejnikov A.V., and Weis K. Yeast poly(A)-binding protein Pab1 shuttles between the nucleus and the cytoplasm and functions in mRNA export. RNA 11 (2005) 517-531
    • (2005) RNA , vol.11 , pp. 517-531
    • Brune, C.1    Munchel, S.E.2    Fischer, N.3    Podtelejnikov, A.V.4    Weis, K.5
  • 8
    • 11844270415 scopus 로고    scopus 로고
    • Yeast poly(A)-binding protein, Pab1, and PAN, a poly(A) nuclease complex recruited by Pab1, connect mRNA biogenesis to export
    • Dunn E.F., Hammell C.M., Hodge C.A., and Cole C.N. Yeast poly(A)-binding protein, Pab1, and PAN, a poly(A) nuclease complex recruited by Pab1, connect mRNA biogenesis to export. Genes Dev 19 (2005) 90-103
    • (2005) Genes Dev , vol.19 , pp. 90-103
    • Dunn, E.F.1    Hammell, C.M.2    Hodge, C.A.3    Cole, C.N.4
  • 10
    • 0035807308 scopus 로고    scopus 로고
    • Quality control of mRNA 3′-end processing is linked to the nuclear exosome
    • Hilleren P., McCarthy T., Rosbash M., Parker R., and Jensen T.H. Quality control of mRNA 3′-end processing is linked to the nuclear exosome. Nature 413 (2001) 538-542
    • (2001) Nature , vol.413 , pp. 538-542
    • Hilleren, P.1    McCarthy, T.2    Rosbash, M.3    Parker, R.4    Jensen, T.H.5
  • 12
    • 9344239333 scopus 로고    scopus 로고
    • A synthetic A tail rescues yeast nuclear accumulation of a ribozyme-terminated transcript
    • Dower K., Kuperwasser N., Merrikh H., and Rosbash M. A synthetic A tail rescues yeast nuclear accumulation of a ribozyme-terminated transcript. RNA 10 (2004) 1888-1899
    • (2004) RNA , vol.10 , pp. 1888-1899
    • Dower, K.1    Kuperwasser, N.2    Merrikh, H.3    Rosbash, M.4
  • 13
    • 7544236961 scopus 로고    scopus 로고
    • Genome-wide mRNA surveillance is coupled to mRNA export
    • The authors of this paper screen the collection of non-essential yeast gene deletion strains for defects in mRNA export and identify lrp1Δ and rrp6Δ. Both are involved in nuclear degradation of mRNA transcripts. They further find that Lrp1 mediates nuclear mRNA degradation in response to DNA damage, a function also mediated by Rrp6. These results provide insights into how mRNA surveillance is coupled with mRNA export.
    • Hieronymus H., Yu M.C., and Silver P.A. Genome-wide mRNA surveillance is coupled to mRNA export. Genes Dev 18 (2004) 2652-2662. The authors of this paper screen the collection of non-essential yeast gene deletion strains for defects in mRNA export and identify lrp1Δ and rrp6Δ. Both are involved in nuclear degradation of mRNA transcripts. They further find that Lrp1 mediates nuclear mRNA degradation in response to DNA damage, a function also mediated by Rrp6. These results provide insights into how mRNA surveillance is coupled with mRNA export.
    • (2004) Genes Dev , vol.18 , pp. 2652-2662
    • Hieronymus, H.1    Yu, M.C.2    Silver, P.A.3
  • 14
    • 27644457087 scopus 로고    scopus 로고
    • A nuclear surveillance pathway for mRNAs with defective polyadenylation
    • Milligan L., Torchet C., Allmang C., Shipman T., and Tollervey D. A nuclear surveillance pathway for mRNAs with defective polyadenylation. Mol Cell Biol 25 (2005) 9996-10004
    • (2005) Mol Cell Biol , vol.25 , pp. 9996-10004
    • Milligan, L.1    Torchet, C.2    Allmang, C.3    Shipman, T.4    Tollervey, D.5
  • 15
    • 19344367418 scopus 로고    scopus 로고
    • Formation of export-competent mRNP: escaping nuclear destruction
    • Saguez C., Olesen J.R., and Jensen T.H. Formation of export-competent mRNP: escaping nuclear destruction. Curr Opin Cell Biol 17 (2005) 287-293
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 287-293
    • Saguez, C.1    Olesen, J.R.2    Jensen, T.H.3
  • 16
    • 0035022577 scopus 로고    scopus 로고
    • A block to mRNA nuclear export in S. cerevisiae leads to hyperadenylation of transcripts that accumulate at the site of transcription
    • Jensen T.H., Patricio K., McCarthy T., and Rosbash M. A block to mRNA nuclear export in S. cerevisiae leads to hyperadenylation of transcripts that accumulate at the site of transcription. Mol Cell 7 (2001) 887-898
    • (2001) Mol Cell , vol.7 , pp. 887-898
    • Jensen, T.H.1    Patricio, K.2    McCarthy, T.3    Rosbash, M.4
  • 17
    • 0742304306 scopus 로고    scopus 로고
    • Nuclear retention of unspliced mRNAs in yeast is mediated by perinuclear Mlp1
    • Galy V., Gadal O., Fromont-Racine M., Romano A., Jacquier A., and Nehrbass U. Nuclear retention of unspliced mRNAs in yeast is mediated by perinuclear Mlp1. Cell 116 (2004) 63-73
    • (2004) Cell , vol.116 , pp. 63-73
    • Galy, V.1    Gadal, O.2    Fromont-Racine, M.3    Romano, A.4    Jacquier, A.5    Nehrbass, U.6
  • 18
    • 15444368318 scopus 로고    scopus 로고
    • Perinuclear Mlp proteins downregulate gene expression in response to a defect in mRNA export
    • Vinciguerra P., Iglesias N., Camblong J., Zenklusen D., and Stutz F. Perinuclear Mlp proteins downregulate gene expression in response to a defect in mRNA export. EMBO J 24 (2005) 813-823
    • (2005) EMBO J , vol.24 , pp. 813-823
    • Vinciguerra, P.1    Iglesias, N.2    Camblong, J.3    Zenklusen, D.4    Stutz, F.5
  • 19
    • 27644511335 scopus 로고    scopus 로고
    • Pml39, a novel protein of the nuclear periphery required for nuclear retention of improper messenger ribonucleoparticles
    • Palancade B., Zuccolo M., Loeillet S., Nicolas A., and Doye V. Pml39, a novel protein of the nuclear periphery required for nuclear retention of improper messenger ribonucleoparticles. Mol Biol Cell 16 (2005) 5258-5268
    • (2005) Mol Biol Cell , vol.16 , pp. 5258-5268
    • Palancade, B.1    Zuccolo, M.2    Loeillet, S.3    Nicolas, A.4    Doye, V.5
  • 20
    • 0037417959 scopus 로고    scopus 로고
    • The C-terminal domain of myosin-like protein 1 (Mlp1p) is a docking site for heterogeneous nuclear ribonucleoproteins that are required for mRNA export
    • Green D.M., Johnson C.P., Hagan H., and Corbett A.H. The C-terminal domain of myosin-like protein 1 (Mlp1p) is a docking site for heterogeneous nuclear ribonucleoproteins that are required for mRNA export. Proc Natl Acad Sci USA 100 (2003) 1010-1015
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 1010-1015
    • Green, D.M.1    Johnson, C.P.2    Hagan, H.3    Corbett, A.H.4
  • 21
    • 8644262258 scopus 로고    scopus 로고
    • Importin beta: conducting a much larger cellular symphony
    • Harel A., and Forbes D.J. Importin beta: conducting a much larger cellular symphony. Mol Cell 16 (2004) 319-330
    • (2004) Mol Cell , vol.16 , pp. 319-330
    • Harel, A.1    Forbes, D.J.2
  • 22
    • 0030911425 scopus 로고    scopus 로고
    • Mex67p, a novel factor for nuclear mRNA export, binds to both poly(A)+ RNA and nuclear pores
    • Segref A., Sharma K., Doye V., Hellwig A., Huber J., Luhrmann R., and Hurt E. Mex67p, a novel factor for nuclear mRNA export, binds to both poly(A)+ RNA and nuclear pores. EMBO J 16 (1997) 3256-3271
    • (1997) EMBO J , vol.16 , pp. 3256-3271
    • Segref, A.1    Sharma, K.2    Doye, V.3    Hellwig, A.4    Huber, J.5    Luhrmann, R.6    Hurt, E.7
  • 23
    • 0033602460 scopus 로고    scopus 로고
    • Movement of nuclear poly(A) RNA throughout the interchromatin space in living cells
    • Politz J.C., Tuft R.A., Pederson T., and Singer R.H. Movement of nuclear poly(A) RNA throughout the interchromatin space in living cells. Curr Biol 9 (1999) 285-291
    • (1999) Curr Biol , vol.9 , pp. 285-291
    • Politz, J.C.1    Tuft, R.A.2    Pederson, T.3    Singer, R.H.4
  • 26
    • 0027211758 scopus 로고
    • Evidence for channeled diffusion of pre-mRNAs during nuclear RNA transport in metazoans
    • Zachar Z., Kramer J., Mims I.P., and Bingham P.M. Evidence for channeled diffusion of pre-mRNAs during nuclear RNA transport in metazoans. J Cell Biol 121 (1993) 729-742
    • (1993) J Cell Biol , vol.121 , pp. 729-742
    • Zachar, Z.1    Kramer, J.2    Mims, I.P.3    Bingham, P.M.4
  • 27
    • 14044266853 scopus 로고    scopus 로고
    • Gene recruitment of the activated INO1 locus to the nuclear membrane
    • The INO1 gene relocalizes to the nuclear periphery upon transcriptional activation, and this requires the activator Hac1 and the integral membrane proteins Scs2. In a strain lacking Scs2, INO1 was still activated if another method was used to recruit the INO1 gene to the nuclear periphery.
    • Brickner J.H., and Walter P. Gene recruitment of the activated INO1 locus to the nuclear membrane. PLoS Biol 2 (2004) 1843-1853. The INO1 gene relocalizes to the nuclear periphery upon transcriptional activation, and this requires the activator Hac1 and the integral membrane proteins Scs2. In a strain lacking Scs2, INO1 was still activated if another method was used to recruit the INO1 gene to the nuclear periphery.
    • (2004) PLoS Biol , vol.2 , pp. 1843-1853
    • Brickner, J.H.1    Walter, P.2
  • 28
    • 18844412748 scopus 로고    scopus 로고
    • Developmentally induced changes in transcriptional program alter spatial organization across chromosomes
    • This paper examines the effects of ∝-factor treatment on gene expression and the intranuclear location of genes. The authors report that ∝-factor-induced genes relocalize to the nuclear periphery. In addition, these genes become associated with Mlp1 in an RNA-dependent manner. Finally, analysis of genes on chromosome III indicates that association with components of NPCs could be mapped to specific locations within the chromosome, including the 3′ ends of activated genes.
    • Casolari J.M., Brown C.R., Drubin D.A., Rando O.J., and Silver P.A. Developmentally induced changes in transcriptional program alter spatial organization across chromosomes. Genes Dev 19 (2005) 1188-1198. This paper examines the effects of ∝-factor treatment on gene expression and the intranuclear location of genes. The authors report that ∝-factor-induced genes relocalize to the nuclear periphery. In addition, these genes become associated with Mlp1 in an RNA-dependent manner. Finally, analysis of genes on chromosome III indicates that association with components of NPCs could be mapped to specific locations within the chromosome, including the 3′ ends of activated genes.
    • (2005) Genes Dev , vol.19 , pp. 1188-1198
    • Casolari, J.M.1    Brown, C.R.2    Drubin, D.A.3    Rando, O.J.4    Silver, P.A.5
  • 30
    • 31544471808 scopus 로고    scopus 로고
    • Nup-PI: the nucleopore-promoter interaction of genes in yeast
    • The authors of this paper define the requirements for interaction of activated genes with the nuclear periphery. Specifically, association is found to require the promoter (the UAS and TATA box) but not the SAGA complex or active transcription.
    • Schmid M., Arib G., Laemmli C., Nishikawa J., Durussel T., and Laemmli U.K. Nup-PI: the nucleopore-promoter interaction of genes in yeast. Mol Cell 21 (2006) 379-391. The authors of this paper define the requirements for interaction of activated genes with the nuclear periphery. Specifically, association is found to require the promoter (the UAS and TATA box) but not the SAGA complex or active transcription.
    • (2006) Mol Cell , vol.21 , pp. 379-391
    • Schmid, M.1    Arib, G.2    Laemmli, C.3    Nishikawa, J.4    Durussel, T.5    Laemmli, U.K.6
  • 31
    • 0035912782 scopus 로고    scopus 로고
    • Assembly and transport of a premessenger RNP particle
    • Daneholt B. Assembly and transport of a premessenger RNP particle. Proc Natl Acad Sci USA 98 (2001) 7012-7017
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 7012-7017
    • Daneholt, B.1
  • 32
    • 4444284306 scopus 로고    scopus 로고
    • Imaging of single-molecule translocation through nuclear pore complexes
    • Through utilization of a nuclear localization sequence fused to two green fluorescent proteins and single molecule fluorescence microscopy, the authors monitor transit of the reporter through the nuclear pore complex (NPC). Importantly, they find that the cargo spends most of its time during the brief period of transit moving randomly within the central channel of the NPC, and that the rate-limiting step for translocation is escape from the NPC. The average duration of interaction of this tagged protein with an NPC is 10 ms.
    • Yang W., Gelles J., and Musser S.M. Imaging of single-molecule translocation through nuclear pore complexes. Proc Natl Acad Sci USA 101 (2004) 12887-12892. Through utilization of a nuclear localization sequence fused to two green fluorescent proteins and single molecule fluorescence microscopy, the authors monitor transit of the reporter through the nuclear pore complex (NPC). Importantly, they find that the cargo spends most of its time during the brief period of transit moving randomly within the central channel of the NPC, and that the rate-limiting step for translocation is escape from the NPC. The average duration of interaction of this tagged protein with an NPC is 10 ms.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 12887-12892
    • Yang, W.1    Gelles, J.2    Musser, S.M.3
  • 33
    • 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., and 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 (1999) 5778-5788
    • (1999) EMBO J , vol.18 , pp. 5778-5788
    • Hodge, C.A.1    Colot, H.V.2    Stafford, P.3    Cole, C.N.4
  • 35
    • 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., and Cole C.N. Dbp5p/Rat8p is a yeast nuclear pore-associated DEAD-box protein essential for RNA export. EMBO J 17 (1998) 2663-2676
    • (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
  • 36
    • 0032079407 scopus 로고    scopus 로고
    • Dbp5p, a cytosolic RNA helicase, is required for poly(A)+ RNA export
    • Tseng S.S., Weaver P.L., Liu Y., Hitomi M., Tartakoff A.M., and Chang T.H. Dbp5p, a cytosolic RNA helicase, is required for poly(A)+ RNA export. EMBO J 17 (1998) 2651-2662
    • (1998) EMBO J , vol.17 , pp. 2651-2662
    • Tseng, S.S.1    Weaver, P.L.2    Liu, Y.3    Hitomi, M.4    Tartakoff, A.M.5    Chang, T.H.6
  • 37
    • 1542344429 scopus 로고    scopus 로고
    • DEAD-box proteins: the driving forces behind RNA metabolism
    • Rocak S., and Linder P. DEAD-box proteins: the driving forces behind RNA metabolism. Nat Rev Mol Cell Biol 5 (2004) 232-241
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 232-241
    • Rocak, S.1    Linder, P.2
  • 38
    • 2342443461 scopus 로고    scopus 로고
    • Protein displacement by DExH/D "RNA helicases" without duplex unwinding
    • Using purified Ded1 and NPH-II, two DExD/H-box helicases that perform different functions, the authors show that these RNA helicases can remove bound protein from RNA, independent of rearrangement of RNA secondary structure. They also find that Ded1 cannot remove NPH-II's protein substrate, TRAP, from bound RNA, further suggesting that DExD/H-box helicases possess some level of functional selectivity.
    • Fairman M.E., Maroney P.A., Wang W., Bowers H.A., Gollnick P., Nilsen T.W., and Jankowsky E. Protein displacement by DExH/D "RNA helicases" without duplex unwinding. Science 304 (2004) 730-734. Using purified Ded1 and NPH-II, two DExD/H-box helicases that perform different functions, the authors show that these RNA helicases can remove bound protein from RNA, independent of rearrangement of RNA secondary structure. They also find that Ded1 cannot remove NPH-II's protein substrate, TRAP, from bound RNA, further suggesting that DExD/H-box helicases possess some level of functional selectivity.
    • (2004) Science , vol.304 , pp. 730-734
    • Fairman, M.E.1    Maroney, P.A.2    Wang, W.3    Bowers, H.A.4    Gollnick, P.5    Nilsen, T.W.6    Jankowsky, E.7
  • 39
    • 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., and Pyle A.M. Active disruption of an RNA-protein interaction by a DExH/D RNA helicase. Science 291 (2001) 121-125
    • (2001) Science , vol.291 , pp. 121-125
    • Jankowsky, E.1    Gross, C.H.2    Shuman, S.3    Pyle, A.M.4
  • 41
    • 0031467708 scopus 로고    scopus 로고
    • A structure/function analysis of Rat7p/Nup159p, an essential nucleoporin of Saccharomyces cerevisiae
    • Del Priore V., Heath C., Snay C., MacMillan A., Gorsch L., Dagher S., and Cole C. A structure/function analysis of Rat7p/Nup159p, an essential nucleoporin of Saccharomyces cerevisiae. J Cell Sci 110 (1997) 2987-2999
    • (1997) J Cell Sci , vol.110 , pp. 2987-2999
    • Del Priore, V.1    Heath, C.2    Snay, C.3    MacMillan, A.4    Gorsch, L.5    Dagher, S.6    Cole, C.7
  • 42
    • 0034695924 scopus 로고    scopus 로고
    • The yeast nuclear pore complex: composition, architecture, and transport mechanism
    • Rout M.P., Aitchison J.D., Suprapto A., Hjertaas K., Zhao Y., and Chait B.T. The yeast nuclear pore complex: composition, architecture, and transport mechanism. J Cell Biol 148 (2000) 635-651
    • (2000) J Cell Biol , vol.148 , pp. 635-651
    • Rout, M.P.1    Aitchison, J.D.2    Suprapto, A.3    Hjertaas, K.4    Zhao, Y.5    Chait, B.T.6
  • 43
    • 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
    • The authors show that the N-terminal region of Nup159, to which Dbp5 binds, is a seven-bladed β propeller, a structure also found in the metazoan ortholog, NUP214. They demonstrate that Dbp5 binds to blades 5-7. Point mutations that render this association temperature-sensitive result in reduced growth and a block to mRNA export, consistent with earlier findings with a Nup159 mutant lacking its N-terminal third.
    • Weirich C.S., Erzberger J.P., Berger J.M., and 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 (2004) 749-760. The authors show that the N-terminal region of Nup159, to which Dbp5 binds, is a seven-bladed β propeller, a structure also found in the metazoan ortholog, NUP214. They demonstrate that Dbp5 binds to blades 5-7. Point mutations that render this association temperature-sensitive result in reduced growth and a block to mRNA export, consistent with earlier findings with a Nup159 mutant lacking its N-terminal third.
    • (2004) Mol Cell , vol.16 , pp. 749-760
    • Weirich, C.S.1    Erzberger, J.P.2    Berger, J.M.3    Weis, K.4
  • 44
    • 0029047324 scopus 로고
    • A conditional allele of the novel repeat-containing yeast nucleoporin Rat7/Nup159 causes both rapid cessation of mRNA export and reversible clustering of nuclear pore complexes
    • Gorsch L.C., Dockendorff T.C., and Cole C.N. A conditional allele of the novel repeat-containing yeast nucleoporin Rat7/Nup159 causes both rapid cessation of mRNA export and reversible clustering of nuclear pore complexes. J Cell Biol 129 (1995) 939-955
    • (1995) J Cell Biol , vol.129 , pp. 939-955
    • Gorsch, L.C.1    Dockendorff, T.C.2    Cole, C.N.3
  • 45
    • 0029816713 scopus 로고    scopus 로고
    • The product of the Saccharomyces cerevisiae RSS1 gene, identified as a high-copy suppressor of the rat7-1 temperature-sensitive allele of the Rat7/Nup159 nucleoporin, is required for efficient mRNA export
    • Del Priore V., Snay C.A., Bahr A., and Cole C.N. The product of the Saccharomyces cerevisiae RSS1 gene, identified as a high-copy suppressor of the rat7-1 temperature-sensitive allele of the Rat7/Nup159 nucleoporin, is required for efficient mRNA export. Mol Biol Cell 7 (1996) 1601-1621
    • (1996) Mol Biol Cell , vol.7 , pp. 1601-1621
    • Del Priore, V.1    Snay, C.A.2    Bahr, A.3    Cole, C.N.4
  • 46
    • 0029745374 scopus 로고    scopus 로고
    • An RNA-export mediator with an essential nuclear export signal
    • Murphy R., and Wente S.R. An RNA-export mediator with an essential nuclear export signal. Nature 383 (1996) 357-360
    • (1996) Nature , vol.383 , pp. 357-360
    • Murphy, R.1    Wente, S.R.2
  • 47
    • 17044415652 scopus 로고    scopus 로고
    • Modularity within the architecture of the nuclear pore complex
    • Schwartz T.U. Modularity within the architecture of the nuclear pore complex. Curr Opin Struct Biol 15 (2005) 221-226
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 221-226
    • Schwartz, T.U.1
  • 48
    • 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., Fahrenkrog B., Zenklusen D., Rychner E., Kantor J., Rosbach M., and Stutz F. 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 (1999) 5761-5777
    • (1999) EMBO J , vol.18 , pp. 5761-5777
    • Strahm, Y.1    Fahrenkrog, B.2    Zenklusen, D.3    Rychner, E.4    Kantor, J.5    Rosbach, M.6    Stutz, F.7
  • 49
    • 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., and Cole C.N. Yeast heat shock mRNAs are exported through a distinct pathway defined by Rip1p. Genes Dev 11 (1997) 2845-2856
    • (1997) Genes Dev , vol.11 , pp. 2845-2856
    • Saavedra, C.A.1    Hammell, C.M.2    Heath, C.V.3    Cole, C.N.4
  • 50
    • 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
    • This paper defines a role for Nup42 during cellular heat stress. In cells lacking Nup42, both the DEAD-box helicase Dbp5 and the nuclear-pore-associated protein Gle1 show dramatically reduced binding to NPCs following heat shock.
    • Rollenhagen C., Hodge C.A., and 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 (2004) 4869-4879. This paper defines a role for Nup42 during cellular heat stress. In cells lacking Nup42, both the DEAD-box helicase Dbp5 and the nuclear-pore-associated protein Gle1 show dramatically reduced binding to NPCs following heat shock.
    • (2004) Mol Cell Biol , vol.24 , pp. 4869-4879
    • Rollenhagen, C.1    Hodge, C.A.2    Cole, C.N.3
  • 52
    • 10944261830 scopus 로고    scopus 로고
    • Cytoplasmic inositol hexakisphosphate production is sufficient for mediating the Gle1-mRNA export pathway
    • Miller A.L., Suntharalingam M., Johnson S.L., Audhya A., Emr S.D., and Wente S.R. Cytoplasmic inositol hexakisphosphate production is sufficient for mediating the Gle1-mRNA export pathway. J Biol Chem 279 (2004) 51022-51032
    • (2004) J Biol Chem , vol.279 , pp. 51022-51032
    • Miller, A.L.1    Suntharalingam, M.2    Johnson, S.L.3    Audhya, A.4    Emr, S.D.5    Wente, S.R.6
  • 53
    • 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., and Wente S.R. A phospholipase C-dependent inositol polyphosphate kinase pathway required for efficient messenger RNA export. Science 285 (1999) 96-100
    • (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
  • 54
    • 27944474017 scopus 로고    scopus 로고
    • The DEAD-box protein Dbp5p is required to dissociate Mex67p from exported mRNPs at the nuclear rim
    • This paper presents evidence that at least one function of DEAD-box helicase Dbp5 in vivo is the removal of the mRNA export receptor Mex67 from the mRNP following its translocation through the nuclear pore.
    • Lund M.K., and Guthrie C. The DEAD-box protein Dbp5p is required to dissociate Mex67p from exported mRNPs at the nuclear rim. Mol Cell 20 (2005) 645-651. This paper presents evidence that at least one function of DEAD-box helicase Dbp5 in vivo is the removal of the mRNA export receptor Mex67 from the mRNP following its translocation through the nuclear pore.
    • (2005) Mol Cell , vol.20 , pp. 645-651
    • Lund, M.K.1    Guthrie, C.2
  • 55
    • 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., and Daneholt B. The mRNA export factor Dbp5 is associated with Balbiani ring mRNP from gene to cytoplasm. EMBO J 21 (2002) 1177-1187
    • (2002) EMBO J , vol.21 , pp. 1177-1187
    • Zhao, J.1    Jin, S.B.2    Bjorkroth, B.3    Wieslander, L.4    Daneholt, B.5
  • 56
    • 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., and 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 (2003) 1664-1676
    • (2003) Mol Biol Cell , vol.14 , pp. 1664-1676
    • Estruch, F.1    Cole, C.N.2
  • 57
    • 0034719392 scopus 로고    scopus 로고
    • The DExH protein NPH-II is a processive and directional motor for unwinding RNA
    • Jankowsky E., Gross C.H., Shuman S., and Pyle A.M. The DExH protein NPH-II is a processive and directional motor for unwinding RNA. Nature 403 (2000) 447-451
    • (2000) Nature , vol.403 , pp. 447-451
    • Jankowsky, E.1    Gross, C.H.2    Shuman, S.3    Pyle, A.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.