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dc.contributor.authorIzquierdo, José M.-
dc.date.accessioned2008-10-21T14:55:56Z-
dc.date.available2008-10-21T14:55:56Z-
dc.date.issued2008-05-28-
dc.identifier.citationMolecular Biology of the Cell, Vol. 19, Issue 8, 3299-3307, August 2008en_US
dc.identifier.issn1059-1524-
dc.identifier.urihttp://hdl.handle.net/10261/7928-
dc.descriptionSupplementary material availableen_US
dc.description.abstractU2 small nuclear ribonucleoprotein (snRNP) auxiliary factor 65 kDa (U2AF65) is an essential splicing factor in the recognition of the pre-mRNA 3' splice sites during the assembly of the splicing commitment complex. We report here that U2AF65 is proteolyzed during apoptosis. This cleavage is group I or III caspase dependent in a noncanonical single site localized around the aspartic acid128 residue and leads to the separation of the N- and C-terminal parts of U2AF65. The U2AF65 N-terminal fragment mainly accumulates in the nucleus within nuclear bodies (nucleoli-like pattern) and to a much lesser extent in the cytoplasm, whereas the C-terminal fragment is found in the cytoplasm, even in localization studies on apoptosis induction. From a functional viewpoint, the N-terminal fragment promotes Fas exon 6 skipping from a reporter minigene, by acting as a dominant-negative version of U2AF65, whereas the C-terminal fragment has no significant effect. The dominant-negative behavior of the U2AF65 N-terminal fragment can be reverted by U2AF35 overexpression. Interestingly, U2AF65 proteolysis in Jurkat cells on induction of early apoptosis correlates with the down-regulation of endogenous Fas exon 6 inclusion. Thus, these results support a functional link among apoptosis induction, U2AF65 cleavage, and the regulation of Fas alternative splicingen_US
dc.description.sponsorshipThis work was supported by a grant from Fondo de Investigaciones Sanitarias (PI051605). The Centro de Biología Molecular "Severo Ochoa" receives an institutional grant from Fundación Ramón Areces.en_US
dc.format.extent1271802 bytes-
dc.format.extent3495938 bytes-
dc.format.mimetypeapplication/pdf-
dc.format.mimetypeapplication/pdf-
dc.language.isoengen_US
dc.publisherAmerican Society for Cell Biologyen_US
dc.rightsopenAccessen_US
dc.subjectU2AF35en_US
dc.subjectU2AF65en_US
dc.titleFas Splicing Regulation during Early Apoptosis Is Linked to Caspase-mediated Cleavage of U2AF65en_US
dc.typeArtículoen_US
dc.identifier.doi10.1091/mbc.E07-11-1125-
dc.description.peerreviewedPeer revieweden_US
dc.relation.publisherversionhttp://dx.doi.org/10.1091/mbc.E07-11-1125en_US
dc.identifier.e-issn1939-4586-
dc.contributor.funderInstituto de Salud Carlos III-
dc.contributor.funderFundación Ramón Areces-
dc.identifier.funderhttp://dx.doi.org/10.13039/100008054es_ES
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