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Referencias:

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• Shen, H., Kan, J.L., Green, M.R., Arginine-serine-rich domains bound at splicing enhancers contact the branchpoint to promote prespliceosome assembly (2004) Mol. Cell, 13, pp. 367-376
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• Hastings, M.L., Krainer, A.R., Pre-mRNA splicing in the new millennium (2001) Curr. Opin. Cell Biol., 13, pp. 302-309
• Spector, D.L., Fu, X.D., Maniatis, T., Associations between distinct pre-mRNA splicing components and the cell nucleus (1991) EMBO J., 10, pp. 3467-3481
• Caceres, J.F., Misteli, T., Screaton, G.R., Spector, D.L., Krainer, A.R., Role of the modular domains of SR proteins in subnuclear localization and alternative splicing specificity (1997) J. Cell Biol., 138, pp. 225-238
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• Patel, N.A., Insulin regulates alternative splicing of protein kinase C beta II through a phosphatidylinositol 3-kinase-dependent pathway involving the nuclear serine/arginine-rich splicing factor, SRp40, in skeletal muscle cells (2001) J. Biol. Chem., 276, pp. 22648-22654
• Van Der Houven Van Oordt, W., The MKK(3/6)-p38-signaling cascade alters the subcellular distribution of hnRNP A1 and modulates alternative splicing regulation (2000) J. Cell Biol., 149, pp. 307-316
• Xie, J., Lee, J.A., Kress, T.L., Mowry, K.L., Black, D.L., Protein kinase A phosphorylation modulates transport of the polypyrimidine tract-binding protein (2003) Proc. Natl. Acad. Sci. USA, 100, pp. 8776-8781
• Gui, J.F., Lane, W.S., Fu, X.D., A serine kinase regulates intracellular localization of splicing factors in the cell cycle (1994) Nature, 369, pp. 678-682
• Colwill, K., The Clk/Sty protein kinase phosphorylates SR splicing factors and regulates their intranuclear distribution (1996) EMBO J., 15, pp. 265-275
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• Kornblihtt, A.R., The fibronectin gene as a model for splicing and transcription studies (1996) FASEB J., 10, pp. 248-257
• Manabe, R., Oh-e, N., Sekiguchi, K., Alternatively spliced EDA segment regulates fibronectin-dependent cell cycle progression and mitogenic signal transduction (1999) J. Biol. Chem., 274, pp. 5919-5924
• Muro, A.F., Regulated splicing of the fibronectin EDA exon is essential for proper skin wound healing and normal lifespan (2003) J. Cell Biol., 162, pp. 149-160
• Caputi, M., A novel bipartite splicing enhancer modulates the differential processing of the human fibronectin EDA exon (1994) Nucleic Acids Res., 22, pp. 1018-1022
• Lavigueur, A., La Branche, H., Kornblihtt, A.R., Chabot, B., A splicing enhancer in the human fibronectin alternate ED1 exon interacts with SR proteins and stimulates U2 snRNP binding (1993) Genes Dev., 7, pp. 2405-2417
• Blaustein, M., Mammary epithelial-mesenchymal interaction regulates fibronectin alternative splicing via phosphatidylinositol 3-kinase (2004) J. Biol. Chem., 279, pp. 21029-21037
• Bos, J.L., ras oncogenes in human cancer: A review (1989) Cancer Res., 49, pp. 4682-4689
• Oliva, J.L., The P34G mutation reduces the transforming activity of K-Ras and N-Ras in NIH 3T3 cells but not of H-Ras (2004) J. Biol. Chem., 279, pp. 33480-33491
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• Cramer, P., Coupling of transcription with alternative splicing: RNA pol II promoters modulate SF2/ASF and 9G8 effects on an exonic splicing enhancer (1999) Mol. Cell, 4, pp. 251-258
• Kuroyanagi, N., Onogi, H., Wakabayashi, T., Hagiwara, M., Novel SR-protein-specific kinase, SRPK2, disassembles nuclear speckles (1998) Biochem. Biophys. Res. Commun., 242, pp. 357-364
• Gingras, A.C., Kennedy, S.G., O'Leary, M.A., Sonenberg, N., Hay, N., 4E-BP1, a repressor of mRNA translation, is phosphorylated and inactivated by the Akt(PKB) signaling pathway (1998) Genes Dev., 12, pp. 502-513
• Li, X., Shambaugh, M.E., Rottman, F.M., Bokar, J.A., SR proteins Asf/SF2 and 9G8 interact to activate enhancer-dependent intron D splicing of bovine growth hormone pre-mRNA in vitro (2000) RNA, 6, pp. 1847-1858
• Pelisch, F., Blaustein, M., Kornblihtt, A.R., Srebrow, A., Cross-talk between signaling pathways regulates alternative splicing: A novel role for JNK (2005) J. Biol. Chem., 280, pp. 25461-25469
• Matter, N., Herrlich, P., Konig, H., Signal-dependent regulation of splicing via phosphorylation of Sam68 (2002) Nature, 420, pp. 691-695
• Patel, N.A., Molecular and genetic studies imply Akt-mediated signaling promotes protein kinase Cβ11 alternative splicing via phosphorylation of serine/arginine-rich splicing factor SRp40 (2005) J. Biol. Chem., 280, pp. 14302-14309
• Du, K., Peng, Y., Greenbaum, L.E., Haber, B.A., Taub, R., HRS/SRp40-mediated inclusion of the fibronectin EIIIB exon, a possible cause of increased EIIIB expression in proliferating liver (1997) Mol. Cell. Biol., 17, pp. 4096-4104
• Gilbert, W., Guthrie, C., The Glc7p nuclear phosphatase promotes mRNA export by facilitating association of Mex67p with mRNA (2004) Mol. Cell, 13, pp. 201-212
• Sanford, J.R., Ellis, J., Cazalla, D., Caceres, J.F., Reversible phosphorylation differentially affects nuclear and cytoplasmic functions of splicing factor 2/alternative splicing factor (2005) Proc. Natl. Acad. Sci. USA, 102, pp. 15042-15047
• Prasad, J., Colwill, K., Pawson, T., Manley, J.L., The protein kinase Clk/Sty directly modulates SR protein activity: Both hyper- and hypophosphorylation inhibit splicing (1999) Mol. Cell. Biol., 19, pp. 6991-7000
• Cavaloc, Y., Bourgeois, C.F., Kister, L., Stevenin, J., The splicing factors 9G8 and SRp20 transactivate splicing through different and specific enhancers (1999) RNA, 5, pp. 468-483
• Hochbaum, D., Tanos, T., Ribeiro-Neto, F., Altschuler, D., Coso, O.A., Activation of JNK by Epac is independent of its activity as a Rap guanine nucleotide exchanger (2003) J. Biol. Chem., 278, pp. 33738-33746
• Ahmed, N.N., Grimes, H.L., Bellacosa, A., Chan, T.O., Tsichlis, P.N., Transduction of interleukin-2 antiapoptotic and proliferative signals via Akt protein kinase (1997) Proc. Natl. Acad. Sci. USA, 94, pp. 3627-3632
• Denegri, M., Stress-induced nuclear bodies are sites of accumulation of premRNA processing factors (2001) Mol. Biol. Cell, 12, pp. 3502-3514
• Duncan, P.I., Stojdl, D.F., Marius, R.M., Scheit, K.H., Bell, J.C., The Clk2 and Clk3 dual-specificity protein kinases regulate the intranuclear distribution of SR proteins and influence pre-mRNA splicing (1998) Exp. Cell Res., 241, pp. 300-308
• De La Mata, M., A slow RNA polymerase II affects alternative splicing in vivo (2003) Mol. Cell, 12, pp. 525-532

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