dc.creator | Limón Mortés, María Cristina | es |
dc.creator | Mora Santos, María del Mar | es |
dc.creator | Espina Zambrano, Águeda Gema | es |
dc.creator | Pintor Toro, José Antonio | es |
dc.creator | López Román, Antonio | es |
dc.creator | Tortolero García, María Dolores | es |
dc.creator | Romero Portillo, Francisco | es |
dc.date.accessioned | 2017-07-27T11:26:34Z | |
dc.date.available | 2017-07-27T11:26:34Z | |
dc.date.issued | 2008 | |
dc.identifier.citation | Limón Mortés, M.C., Mora Santos, M.d.M., Espina Zambrano, Á.G., Pintor Toro, J.A., López Román, A., Tortolero García, M.D. y Romero Portillo, F. (2008). UV-induced degradation of securin is mediated by SKP1-CUL1-βTrCP E3 ubiquitin ligase. Journal of Cell Science, 121 (11), 1825-1831. | |
dc.identifier.issn | 0021-9533 (impreso) | es |
dc.identifier.issn | 1477-9137 (electronico) | es |
dc.identifier.uri | http://hdl.handle.net/11441/63328 | |
dc.description.abstract | Securin is a chaperone protein with bifunctional properties. It binds to separase to inhibit premature sister chromatid separation until the onset of anaphase, and it also takes part in cell-cycle arrest after UV irradiation. At metaphase-to-anaphase transition, securin is targeted for proteasomal destruction by the anaphase-promoting complex or cyclosome (APC/C),
allowing activation of separase. However, although securin is reported to undergo proteasome-dependent degradation after UV irradiation, the ubiquitin ligase responsible for securing ubiquitylation has not been well characterized. In this study, we show that UV radiation induced a marked reduction of securin in both the nucleus and cytoplasm. Moreover, we show that GSK-3β inhibitors prevent securin degradation, and that
CUL1 and βTrCP are involved in this depletion. We also confirmed that SKP1-CUL1-βTrCP (SCFβTrCP) ubiquitylates securin in vivo, and identified a conserved and unconventional βTrCP recognition motif (DDAYPE) in the securin primary amino acid sequence of humans, nonhuman primates and rodents. Furthermore, downregulation of βTrCP caused an accumulation of securin in non-irradiated cells. We conclude that SCFβTrCP is the E3 ubiquitin ligase responsible for securing degradation after UV irradiation, and that it is involved in securin turnover in nonstressed cells. | es |
dc.description.sponsorship | Ministerio de Educación y Ciencia SAF 2005-07713-C03-01 | es |
dc.format | application/pdf | es |
dc.language.iso | eng | es |
dc.publisher | Company of Biologists | es |
dc.relation.ispartof | Journal of Cell Science, 121 (11), 1825-1831. | |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.subject | Cell cycle | es |
dc.subject | Proteasome | es |
dc.subject | Ubiquitylation | es |
dc.subject | Ultraviolet radiation | es |
dc.subject | Degradation | es |
dc.title | UV-induced degradation of securin is mediated by SKP1-CUL1-βTrCP E3 ubiquitin ligase | es |
dc.type | info:eu-repo/semantics/article | es |
dcterms.identifier | https://ror.org/03yxnpp24 | |
dc.type.version | info:eu-repo/semantics/publishedVersion | es |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | es |
dc.contributor.affiliation | Universidad de Sevilla. Departamento de Microbiología | es |
dc.relation.projectID | SAF 2005-07713-C03-01 | es |
dc.relation.publisherversion | http://dx.doi.org/10.1242/jcs.020552 | es |
dc.identifier.doi | 10.1242/jcs.020552 | es |
idus.format.extent | 7 p. | es |
dc.journaltitle | Journal of Cell Science | es |
dc.publication.volumen | 121 | es |
dc.publication.issue | 11 | es |
dc.publication.initialPage | 1825 | es |
dc.publication.endPage | 1831 | es |
dc.contributor.funder | Ministerio de Educación y Ciencia (MEC). España | |