Fas splicing regulation during early apoptosis is linked to caspase-mediated cleavage of U2AF65

Molecular Biology of the Cell

Volumn 19, Issue 8, 2008, Pages 3299-3307

  Izquierdo, José M ^a  

^a CENTRO DE BIOLOGÍA MOLECULAR SEVERO OCHOA   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; CASPASE 3; FAS ANTIGEN; INTERLEUKIN 1BETA CONVERTING ENZYME; RIBONUCLEOPROTEIN; U2AF65 PROTEIN; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; APOPTOSIS; ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL NUCLEUS INCLUSION BODY; CONTROLLED STUDY; HUMAN; HUMAN CELL; IN VITRO STUDY; LEUKEMIA CELL LINE; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; RNA SPLICING;

EID: 54249164720     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E07-11-1125     Document Type: Article

References (43)

1. Adams, J. M. (2003). Ways of dying: multiple pathways to apoptosis. Genes Dev. 17, 2481-2495.
2. Banerjee, H., Rahn, A., Davis, W., and Singh, R. (2003). Sex-lethal and U2 small nuclear ribonucleoprotein auxiliary factor (U2AF65) recognize polypyrimidine tracts using multiple modes of binding. RNA 9, 88-99.
3. Bidere, N., Su, H. C., and Lenardo, M. J. (2006). Genetic disorders of programmed cell death in the immune system. Annu. Rev. Immunol. 24, 321-352.
4. Buendia, B., Santa-Maria, A., and Courvalin, J. C. (1999). Caspase-dependent proteolysis of integral and peripheral proteins of nuclear membranes and nuclear pore complex proteins during apoptosis. J. Cell Sci. 112, 1743-1753.
5. Cheng, J., Zhou, T., Liu, C., Shapiro, J. P., Brauer, M. J., Kiefer, M. C., Barr, P. J., and Mountz, J. D. (1994). Protection from Fas-mediated apoptosis by a soluble form of the Fas molecule. Science 263, 1759-1762.
6. Danckwardt, S. et al. (2007). Splicing factors stimulate polyadenylation via USEs at non-canonical 3′ end formation signals. EMBO J. 26, 2658-2669.
7. Dignam, J. D., Lebovitz, R. M., and Roeder, R. G. (1983). Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res. 11, 1475-1489.
8. Earnshaw, W. C., Martins, L. M., and Kaufmann, S. H. (1999). Mammalian caspases: structure, activation, substrates, and functions during apoptosis. Annu. Rev. Biochem. 68, 383-424.
9. Elbashir, S. M., Harborth, J., Lendeckel, W., Yalcin, A., Weber, K., and Tuschl, T. (2001). Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells. Nature 411, 494-498.
10. Ferrando-May, E. (2005). Nucleocytoplasmic transport in apoptosis. Cell Death Differ. 12, 1263-1276.
11. Fischer, U., Janicke, R. U., and Schulze-Osthoff, K. (2003). Many cuts to ruin: a comprehensive update of caspase substrates. Cell Death Differ. 10, 76-100.
12. Förch, P., Puig, O., Kedersha, N., Martínez, C., Granneman, S., Seraphin, B., Anderson, P., and Valcárcel, J. (2000). The apoptosis-promoting factor TIA-1 is a regulator of alternative pre-mRNA splicing. Mol. Cell 6, 1089-1098.
13. Gama-Carvalho, M., Carvalho, M. P., Kehlenbach, A., Valcárcel, J., and Carmo-Fonseca, M. (2001). Nucleocytoplasmic shuttling of heterodimeric splicing factor U2AF. J. Biol. Chem. 276, 13104-13112.
14. Gama-Carvalho, M., Krauss, R. D., Chiang, L., Valcárcel, J., Green, M. R., and Carmo-Fonseca, M. (1997). Targeting of U2AF65 to sites of active splicing in the nucleus. J. Cell Biol. 137, 975-987.
15. Gama-Carvalho, M., Barbosa-Morais, N. L., Brodsky, A. S., Silver, P. A., and Carmo-Fonseca, M. (2006). Genome-wide identification of functionally distinct subsets of cellular mRNAs associated with two nucleocytoplasmic shuttling mammalian splicing factors. Genome Biol. 7, R113.
16. He, X., Pool, M., Darcy, K.M., Lim, S.B., Auersperg, N., Coon, J.S., and Beck, W.T. (2007). Knockdown of polypyrimidine tract-binding protein suppresses ovarian tumor cell growth and invasiveness in vitro. Oncogene 26, 4961-4968.
17. Izquierdo, J. M., Majós, N., Bonnal, S., Martínez, C., Castelo, R., Guigo, R., Bilbao, D., and Valcárcel, J. (2005). Regulation of Fas alternative splicing by antagonistic effects of TIA-1 and PTB on exon definition. Mol. Cell 19, 475-484.
18. Izquierdo, J. M., and Valcárcel, J. (2006). A simple principle to explain the evolution of pre-mRNA splicing. Genes Dev. 20, 1679-1684.
19. Izquierdo, J. M., and Valcárcel, J. (2007a). Fas-activated serine/threonine kinase (FAST K) synergizes with TIA-1/TIAR proteins to regulate Fas alternative splicing. J. Biol. Chem. 282, 1539-1543.
20. Izquierdo, J. M., and Valcárcel, J. (2007b). Two isoforms of the T-cell intracellular antigen 1 (TIA-1) splicing factor display distinct splicing regulation activities. Control of TIA-1 isoform ratio by TIA-1-related protein. J. Biol. Chem. 282, 19410-19417.
21. Keene, J. D., and Tenenbaum, S. A. (2002). Eukaryotic mRNPs may represent posttranscriptional operons. Mol. Cell 9, 1161-1167.
22. Krammer, P. H. (2000). CD95's deadly mission in the immune system. Nature 407, 789-795.
23. Lavrik, I. N., Golks, A., and Krammer, P. H. (2005). Caspases: pharmacological manipulation of cell death. J. Clin. Invest. 115, 2665-2672.
24. Leung, A.K.L., and Sharp, P. A. (2006). Function and localization of microRNAs in mammalian cells. Cold Spring Harb. Symp. Quant. Biol. 71, 29-38.
25. Mata, J., Marguerat, S., and Bahler, J. (2005). Post-transcriptional control of gene expression: a genome-wide perspective. Trends Biochem. Sci. 30, 506-514.
26. Merendino, L., Guth, S., Bilbao, D., Martínez, C., and Valcárcel, J. (1999). Inhibition of msl-2 splicing by Sex-lethal reveals interaction between U2AF35 and the 3′ splice site AG. Nature 402, 838-841.
27. Millevoi, S., Loulergue, C., Dettwiler, S., Karaa, S. Z., Keller, W., Antoniou, M., and Vagner, S. (2006). An interaction between U2AF 65 and CF I(m) links the splicing and 3′ end processing machineries. EMBO J 25, 4854-4864.
28. Moore, M. J. (2005). From birth to death: the complex lives of eukaryotic mRNAs. Science 309, 1514-1518.
29. Pacheco, T. R., Coelho, M. B., Desterro, J.M.P., Mollet, I., and Carmo-Fonseca, M. (2006a). In vivo requirement of the small subunit of U2AF for recognition of a weak 3′ splice site. Mol. Cell. Biol. 26, 8183-8190.
30. Pacheco, T. R., Moita, L. F., Gomes, A. Q., Hacohen, N., and Carmo-Fonseca, M. (2006b). RNA interference knockdown of hU2AF35 impairs cell cycle progression and modulates alternative splicing of Cdc25 transcripts. Mol. Biol. Cell 17, 4187-4199.
31. Prasanth, K. V., and Spector, D. L. (2007). Eukaryotic regulatory RNAs: an answer to the "genome complexity" conundrum. Genes Dev. 21, 11-42.
32. Proussakova, O. V., Rabaya, N. A., Moshnikova, A. B., Telegina, E. S., Turanov, A., Nanazashvili, M. G., and Beletsky, I. P. (2003). Oligomerization of soluble Fas antigen induces its cytotoxicity. J. Biol. Chem. 278, 36236-36241.
33. Reed, R. (1989). The organization of 3′ splice-site sequences in mammalian introns. Genes Dev. 3, 2113-2123.
34. Schwerk, C., and Schulze-Osthoff, K. (2005). Regulation of apoptosis by alternative pre-mRNA splicing. Mol. Cell 19, 1-13.
35. Selenko, P., Gregorovic, G., Sprangers, R., Stier, G., Rhani, Z., Kramer, A., and Sattler, M. (2003). Structural basis for the molecular recognition between human splicing factors U2AF65 and SF1/mBBP. Mol. Cell 11, 965-976.
36. Shen, H., and Green, M. R. (2006). RS domains contact splicing signals and promote splicing by a common mechanism in yeast through humans. Genes Dev. 20, 1755-1765.
37. Sickmier, E. A., Frato, K. E., Shen, H., Paranawithana, S. R., Green, M. R., and Kielkopf, C. L. (2006). Structural basis for polypyrimidine tract recognition by the essential pre-mRNA splicing factor U2AF65. Mol. Cell 23, 49-59.
38. Soares, L. M., Zanier, K., Mackereth, C., Sattler, M., and Valcárcel, J. (2006). Intron removal requires proofreading of U2AF/3′ splice site recognition by DEK. Science 312, 1961-1965.
39. Valcárcel, J., Gaur, R. K., Singh, R., and Green, M. R. (1996). Interaction of U2AF65 RS region with pre-mRNA branch point and promotion of base pairing with U2 snRNA. Science 273, 1706-1709.
40. Van Damme, P., Martens, L., Van Damme, J., Hugelier, K., Staes, A., Vandekerckhove, J., and Gevaert, K. (2005). Caspase-specific and nonspecific in vivo protein processing during Fas-induced apoptosis. Nat. Methods 2, 771-777.
41. Wu, S., Romfo, C. M., Nilsen, T. W., and Green, M. R. (1999). Functional recognition of the 3′ splice site AG by the splicing factor U2AF35. Nature 402, 832-835.
42. Zamore, P. D., Patton, J. G., and Green, M. R. (1992). Cloning and domain structure of the mammalian splicing factor U2AF. Nature 355, 609-614.
43. Zorio, D., and Blumenthal, T. (1999). Both subunits of U2AF recognize the 3′ splice site in Caenorhabditis elegans. Nature 402, 835-838.