The interplay of nuclear mRNP assembly, mRNA surveillance and export

Trends in Cell Biology

Volumn 13, Issue 6, 2003, Pages 319-327

  Stutz, Françoise ^a   Izaurralde, Elisa ^b  

^a UNIVERSITY OF GENEVA   (Switzerland)

^b EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; DIMER; MESSENGER RIBONUCLEOPROTEIN; MESSENGER RNA; NUCLEOPORIN; PROTEIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; CYTOPLASM; GENETIC TRANSCRIPTION; HUMAN; MOLECULAR MECHANICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DEGRADATION; PROTEIN DOMAIN; QUALITY CONTROL; REVIEW; RNA SPLICING; SOMATIC CELL GENETICS;

METAZOA;

EID: 0038697629     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0962-8924(03)00106-5     Document Type: Review

References (80)

1. Ryan K., Wente S.R. The nuclear pore complex: a protein machine bridging the nucleus and cytoplasm. Curr. Opin. Cell Biol. 12:2000;361-371.
2. Vasu S.K., Forbes D.J. Nuclear pores and nuclear assembly. Curr. Opin. Cell Biol. 13:2001;363-375.
3. Cullen B.R. Nuclear RNA export. J. Cell Sci. 116:2003;587-597.
4. Herold A., et al. TAP/NXF1 belongs to a multigene family of putative RNA export factors with a conserved modular architecture. Mol. Cell. Biol. 20:2000;8996-9008.
5. Jun L., et al. NXF5, a novel member of the nuclear RNA export factor family, is lost in a male patient with a syndromic form of mental retardation. Curr. Biol. 11:2001;1381-1391.
6. Segref A., et al. Mex67p, a novel factor for nuclear mRNA export binds to both poly(A)+ RNA and nuclear pores. EMBO J. 16:1997;3256-3271.
7. Tan W., et al. The mRNA export in C. elegans is mediated by Ce NXF1, an orthologue of human TAP/NXF1 and S. cerevisiae Mex67p. RNA. 6:2000;1762-1772.
8. Yang J., et al. Two closely related human nuclear export factors utilize entirely distinct export pathways. Mol. Cell. 8:2001;397-406.
9. Katahira J., et al. The Mex67p-mediated nuclear mRNA export pathway is conserved from yeast to human. EMBO J. 18:1999;2593-2609.
10. Herold A., et al. NXF1/p15 heterodimers are essential for mRNA nuclear export in Drosophila. RNA. 7:2001;1768-1780.
11. Hurt E., et al. Mex67p mediates nuclear export of a variety of RNA polymerase II transcripts. J. Biol. Chem. 275:2000;8361-8365.
12. Vainberg I.E., et al. Nuclear export of heat shock and non-heat-shock mRNA occurs via similar pathways. Mol. Cell. Biol. 20:2000;3996-4005.
13. Wilkie G.S., et al. Small bristles, the Drosophila ortholog of human TAP/NXF1 and yeast Mex67p, is essential for mRNA nuclear export in all tissues throughout development. RNA. 7:2001;1781-1792.
14. Grüter P., et al. TAP, the human homolog of Mex67p, mediates CTE-dependent RNA export from the nucleus. Mol. Cell. 1:1998;649-659.
15. Braun I.C., et al. Overexpression of TAP/p15 heterodimers bypasses nuclear retention and stimulates nuclear mRNA export. J. Biol. Chem. 276:2001;20536-20543.
16. Guzik B.W., et al. NXT1 (p15) is a crucial cellular cofactor in TAP-dependent export of intron-containing RNA in mammalian cells. Mol. Cell. Biol. 21:2001;2545-2554.
17. Yoon J.H., et al. Mex67p of Schizosaccharomyces pombe interacts with Rae1p in mediating mRNA export. Mol. Cell. Biol. 20:2000;8767-8782.
18. Fribourg S., et al. Structural basis for the recognition of a nucleoporin FG repeat by the NTF2-like domain of the TAP/p15 mRNA nuclear export factor. Mol. Cell. 8:2001;645-656.
19. Wiegand H.L., et al. Formation of Tap/NXT1 heterodimers activates tap-dependent nuclear mRNA export by enhancing recruitment to nuclear pore complexes. Mol. Cell. Biol. 22:2002;245-256.
20. Santos-Rosa H., et al. Nuclear mRNA export requires complex formation between Mex67p and Mtr2p at the nuclear pores. Mol. Cell. Biol. 18:1998;6826-6838.
21. Strässer K., et al. Binding of the Mex67p/Mtr2p heterodimer to FXFG, GLFG, and FG repeat nucleoporins is essential for nuclear mRNA export. J. Cell Biol. 150:2000;695-706.
22. Liker E., et al. The structure of the mRNA nuclear export factor TAP reveals a cis arrangement of a non-canonical RNP domain and a leucine-rich-repeat domain. EMBO J. 19:2000;5587-5598.
23. Grant R.P., et al. Structural basis for the interaction between the Tap C-terminal domain and FG repeat-containing nucleoporins. Nat. Struct. Biol. 4:2002;247-251.
24. Grant R.P., et al. structural basis for the interaction between the Tap/NXF1 UBA domain and FG nucleoporins at 1A resolution. J. Mol. Biol. 326:2003;849-858.
25. Bachi A., et al. The C-terminal domain of TAP interacts with the nuclear pore complex and promotes export of specific CTE-bearing RNA substrates. RNA. 6:2000;136-158.
26. Braun I.C., et al. Nuclear export of messenger RNA by TAP/NXF1 requires two nucleoporin binding sites but not p15. Mol. Cell. Biol. 22:2002;5405-5418.
27. Bayliss R., et al. Structural basis for the interaction between FxFG nucleoporin repeats and importin β in nuclear trafficking. Cell. 102:2000;99-108.
28. Bayliss R., et al. Structural basis for the interaction between NTF2 and nucleoporin FxFG repeats. EMBO J. 21:2002;2843-2853.
29. Ribbeck K., Görlich D. The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion. EMBO J. 21:2002;2664-2671.
30. Dreyfuss G., et al. Messenger-RNA-binding proteins and the messages they carry. Nat. Rev. Mol. Cell Biol. 3:2002;195-205.
31. Stutz F., et al. REF, an evolutionary conserved family of hnRNP-like proteins, interacts with TAP/Mex67p and participates in mRNA nuclear export. RNA. 6:2000;638-650.
32. Strässer K., Hurt E. Yra1p, a conserved nuclear RNA-binding protein, interacts directly with Mex67p and is required for mRNA export. EMBO J. 19:2000;410-420.
33. Zenklusen D., et al. The yeast hnRNP-Like proteins Yra1p and Yra2p participate in mRNA export through interaction with Mex67p. Mol. Cell. Biol. 21:2001;4219-4232.
34. Lei E.P., et al. Messenger RNAs are recruited for nuclear export during transcription. Genes Dev. 15:2001;1771-1782.
35. Lei E.P., Silver P.A. Intron status and 3′-end formation control cotranscriptional export of mRNA. Genes Dev. 16:2002;2761-2766.
36. Hieronymus H., Silver P.A. Genome-wide analysis of RNA-protein interactions illustrates specificity of the mRNA export machinery. Nat. Genet. 33:2003;155-161.
37. Rodrigues J.P., et al. REF proteins mediate the export of spliced and unspliced mRNAs from the nucleus. Proc. Natl. Acad. Sci. U. S. A. 98:2001;1030-1035.
38. Zhou Z., et al. The protein Aly links pre-messenger-RNA splicing to nuclear export in metazoans. Nature. 407:2000;401-405.
39. Koffa M., et al. Herpes simplex virus ICP27 protein provides viral mRNAs with access to the cellular mRNA export pathway. EMBO J. 20:2001;5769-5778.
40. Chen I.H., et al. ICP27 interacts with the RNA export factor Aly/REF to direct herpes simplex virus type 1 intronless mRNAs to the TAP export pathway. J. Virol. 76:2002;12877-12889.
41. Hiriart E., et al. A novel nuclear export signal and a REF interaction domain both promote mRNA export by the Epstein-Barr virus EB2 protein. J. Biol. Chem. 278:2003;335-342.
42. Gatfield D., Izaurralde E. REF1/Aly and the additional exon junction complex proteins are dispensable for nuclear mRNA export. J. Cell Biol. 159:2002;579-588.
43. Zenklusen D., et al. Stable mRNP formation and export require cotranscriptional recruitment of the mRNA export factors Yra1p and Sub2p by Hpr1p. Mol. Cell. Biol. 22:2002;8241-8253.
44. Jensen T.H., et al. The DECD box putative ATPase Sub2p is an early mRNA export factor. Curr. Biol. 11:2001;1711-1715.
45. Libri D., et al. Interactions between mRNA export commitment, 3′-end quality control, and nuclear degradation. Mol. Cell. Biol. 22:2002;8254-8266.
46. Strässer K., Hurt E. Splicing factor Sub2p is required for nuclear mRNA export through its interaction with Yra1p. Nature. 413:2001;648-652.
47. Strässer K., et al. TREX is a conserved complex coupling transcription with messenger RNA export. Nature. 417:2002;304-308.
48. Linder P., Stutz F. mRNA export: travelling with DEAD box proteins. Curr. Biol. 11:2001;R961-R963.
49. Gatfield D., et al. The DExH/D-box protein HEL/UAP56 is essential for mRNA nuclear export in Drosophila. Curr. Biol. 11:2001;1716-1721.
50. Luo M.L., et al. Pre-mRNA splicing and mRNA export linked by direct interactions between UAP56 and Aly. Nature. 413:2001;644-647.
51. Kiesler E., et al. HEL/UAP56 binds cotranscriptionally to the Balbiani ring pre-mRNA in an intron-independent manner and accompanies the BR mRNP to the nuclear pore. Curr. Biol. 12:2002;859-862.
52. Le Hir, H. et al. How introns influence and enhance eukaryotic gene expression. Trends Biochem. Sci. (in press).
53. Luo M.J., Reed R. Splicing is required for rapid and efficient mRNA export in metazoans. Proc. Natl. Acad. Sci. U. S. A. 96:1999;14937-14942.
54. Le Hir H., et al. The exon-exon junction complex provides a binding platform for factors involved in mRNA export and NMD. EMBO J. 20:2001;4987-4997.
55. Ohno M., et al. Identity elements used in export of mRNAs. Mol. Cell. 9:2002;659-671.
56. Zhou Z., et al. The protein Aly links pre-messenger-RNA splicing to nuclear export in metazoans. Nature. 407:2000;401-405.
57. Le Hir H., et al. The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions. EMBO J. 19:2000;6860-6869.
58. Kataoka N., et al. Magoh, a human homolog of Drosophila mago nashi protein, is a component of the splicing-dependent exon-exon junction complex. EMBO J. 20:2001;6424-6433.
59. Lu, S. and Cullen, B.R. Analysis of the stimulatory effect of splicing on mRNA production and utilization in mammalian cells. Mol. Cell. Biol. (in press).
60. Nott, A. et al. Quantitative analysis of intron effects on mammalian gene expression reveals enhanced polysome association of spliced mRNAs. Mol. Cell. Biol. (in press).
61. Jensen T.H., Rosbash M. Cotranscriptional monitoring of mRNP formation. Nat. Struct. Biol. 10:2003;10-12.
62. Chavez S., et al. A protein complex containing Tho2, Hpr1, Mft1 and a novel protein, Thp2, connects transcription elongation with mitotic recombination in Saccharomyces cerevisiae. EMBO J. 19:2000;5824-5834.
63. Chang M., et al. A complex containing RNA polymerase II, Paf1p, Cdc73p, Hpr1p, and Ccr4p plays a role in protein kinase C signaling. Mol. Cell. Biol. 19:1999;1056-1067.
64. Pokholok D.K., et al. Exchange of RNA polymerase II initiation and elongation factors during gene expression in vivo. Mol. Cell. 9:2002;799-809.
65. West R.W. Jr, et al. RLR1 (THO2), required for expressing lacZ fusions in yeast, is conserved from yeast to humans and is a suppressor of SIN4. Gene. 243:2000;195-205.
66. Butler J.S. The yin and yang of the exosome. Trends Cell Biol. 12:2002;90-96.
67. Bousquet-Antonelli C., et al. Identification of a regulated pathway for nuclear pre-mRNA turnover. Cell. 102:2000;765-775.
68. Burkard K.T., Butler J.S. A nuclear 3′-5′ exonuclease involved in mRNA degradation interacts with poly(A) polymerase and the hnRNA protein Npl3p. Mol. Cell. Biol. 20:2000;604-616.
69. Torchet C., et al. Processing of 3′-extended read-through transcripts by the exosome can generate functional mRNAs. Mol. Cell. 9:2002;1285-1296.
70. Brodsky A.S., Silver P.A. Pre-mRNA processing factors are required for nuclear export. RNA. 6:2000;1737-1749.
71. Hammell C.M., et al. Coupling of termination, 3′ processing, and mRNA export. Mol. Cell. Biol. 22:2002;6441-6457.
72. Dower K., Rosbash M. T7 RNA polymerase-directed transcripts are processed in yeast and link 3′ end formation to mRNA nuclear export. RNA. 8:2002;686-697.
73. Hilleren P., et al. Quality control of mRNA 3′-end processing is linked to the nuclear exosome. Nature. 413:2001;538-542.
74. Jensen T.H., et al. 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.
75. Herold, A. et al. Genome-wide analysis of nuclear mRNA export pathways in Drosophila. EMBO J. (in press).
76. Andrulis E.D., et al. The RNA processing exosome is linked to elongating RNA polymerase II in Drosophila. Nature. 420:2002;837-841.
77. Chavez S., et al. Hpr1 is preferentially required for transcription of either long or G+C-rich DNA sequences in Saccharomyces cerevisiae. Mol. Cell. Biol. 21:2001;7054-7064.
78. Portman D.S., et al. YRA1, an essential Saccharomyces cerevisiae gene, encodes a novel nuclear protein with RNA annealing activity. RNA. 3:1997;527-537.
79. Piruat J.I., Aguilera A. A novel yeast gene, THO2, is involved in RNA pol II transcription and provides new evidence for transcriptional elongation-associated recombination. EMBO J. 17:1998;4859-4872.
80. Saitou N., Nei M. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4:1987;406-425.