2024-03-29T12:31:33Zhttp://digital.csic.es/dspace-oai/requestoai:digital.csic.es:10261/33522021-12-27T15:36:27Zcom_10261_15com_10261_6col_10261_268
DIGITAL.CSIC
author
Romero, Francisco
author
Gil-Bernabé, Ana M.
author
Sáez, Carmen
author
Japón, Miguel A.
author
Pintor-Toro, José Antonio
author
Tortolero, María
funder
Ministerio de Ciencia y Tecnología (España)
funder
Junta de Andalucía
funder
Instituto de Salud Carlos III
funder
Asociación de Padres de Niños con Cáncer de Andalucía
2008-03-28T08:14:18Z
2008-03-28T08:14:18Z
2004
Molecular and Cellular Biology 24(7): 2720–2733 (2004)
1098-5549
http://hdl.handle.net/10261/3352
10.1128/MCB.24.7.2720-2733.2004
http://dx.doi.org/10.13039/501100006280http://dx.doi.org/10.13039/501100004587http://dx.doi.org/10.13039/501100011011
15024062
All eukaryotic cells possess elaborate mechanisms to protect genome integrity and ensure survival after DNA
damage, ceasing proliferation and granting time for DNA repair. Securin is an inhibitory protein that is bound
to a protease called Separase to inhibit sister chromatid separation until the onset of anaphase. At the
metaphase-to-anaphase transition, Securin is degraded by the anaphase-promoting complex or cyclosome, and
Separase contributes to the release of cohesins from the chromosome, allowing for the segregation of sister
chromatids to opposite spindle poles. Here we provide evidence that human Securin (hSecurin) has a novel role
in cell cycle arrest after exposure to UV light or ionizing radiation. In fact, irradiation downregulated the level
of hSecurin protein, accelerating its degradation via the proteasome and reducing hSecurin mRNA translation,
but the presence of hSecurin is necessary for cell proliferation arrest following UV treatment. Moreover, an
alteration of UV-induced hSecurin downregulation could lead directly to the accumulation of DNA damage and
the subsequent development of malignant tumors.
eng
closedAccess
Securin Is a Target of the UV Response Pathway in Mammalian Cells
artículo
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