Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/114000
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Campo DC | Valor | Lengua/Idioma |
---|---|---|
dc.contributor.author | Pérez, Moisés | - |
dc.contributor.author | García-Limones, Carmen | - |
dc.contributor.author | Zapico, Inés | - |
dc.contributor.author | Marina, Anabel | - |
dc.contributor.author | Schmitz, M. Lienhard | - |
dc.contributor.author | Muñoz, Eduardo | - |
dc.contributor.author | Calzado, Marco A. | - |
dc.date.accessioned | 2015-04-22T11:29:01Z | - |
dc.date.available | 2015-04-22T11:29:01Z | - |
dc.date.issued | 2012 | - |
dc.identifier | doi: 10.1093/jmcb/mjs047 | - |
dc.identifier | issn: 1674-2788 | - |
dc.identifier.citation | Journal of Molecular Cell Biology 4: 316- 330 (2012) | - |
dc.identifier.uri | http://hdl.handle.net/10261/114000 | - |
dc.description.abstract | The ubiquitin E3 ligase SIAH2 is an important regulator of the hypoxic response as it leads to the ubiquitin/proteasomal degradation of prolyl hydroxylases such as PHD3, which in turn increases the stability of hypoxia-inducible factor (HIF)-1α. In the present study, we identify the serine/threonine kinase DYRK2 as SIAH2 interaction partner that phosphorylates SIAH2 at five residues (Ser16, Thr26, Ser28, Ser68, and Thr119). Phosphomimetic and phospho-mutant forms of SIAH2 exhibit different subcellular localizations and consequently change in PHD3 degrading activity. Accordingly, phosphorylated SIAH2 is more active than the wild-type E3 ligase and shows an increased ability to trigger the HIF-1α-mediated transcriptional response and angiogenesis. We also found that SIAH2 knockdown increases DYRK2 stability, whereas SIAH2 expression facilitates DYRK2 polyubiquitination and degradation. Hypoxic conditions cause a SIAH2-dependent DYRK2 polyubiquitination and degradation which ultimately also results in an impaired SIAH2 phosphorylation. Similarly, DYRK2-mediated phosphorylation of p53 at Ser46 is impaired under hypoxic conditions, suggesting a molecular mechanism underlying chemotherapy resistance in solid tumors. © 2012 The Author (2012). Published by Oxford University Press on behalf of Journal of Molecular Cell Biology, IBCB, SIBS, CAS. All rights reserved. | - |
dc.description.sponsorship | MICINN (SAF2010-17122); Consejería de Salud (Junta de Andalucía) | - |
dc.publisher | Oxford University Press | - |
dc.rights | closedAccess | - |
dc.subject | Ubiquitination | - |
dc.subject | Phosphorylation | - |
dc.subject | Hypoxia | - |
dc.subject | DYRK2 | - |
dc.subject | SIAH2 | - |
dc.title | Mutual regulation between SIAH2 and DYRK2 controls hypoxic and genotoxic signaling pathways | - |
dc.type | artículo | - |
dc.identifier.doi | 10.1093/jmcb/mjs047 | - |
dc.date.updated | 2015-04-22T11:29:02Z | - |
dc.description.version | Peer Reviewed | - |
dc.language.rfc3066 | eng | - |
dc.contributor.funder | Ministerio de Economía y Competitividad (España) | - |
dc.contributor.funder | Junta de Andalucía | - |
dc.identifier.funder | http://dx.doi.org/10.13039/501100003329 | es_ES |
dc.identifier.funder | http://dx.doi.org/10.13039/501100011011 | es_ES |
dc.type.coar | http://purl.org/coar/resource_type/c_6501 | es_ES |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.fulltext | No Fulltext | - |
item.cerifentitytype | Publications | - |
item.openairetype | artículo | - |
item.grantfulltext | none | - |
Aparece en las colecciones: | (CBM) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
accesoRestringido.pdf | 15,38 kB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
SCOPUSTM
Citations
48
checked on 01-abr-2024
WEB OF SCIENCETM
Citations
48
checked on 27-feb-2024
Page view(s)
305
checked on 16-abr-2024
Download(s)
86
checked on 16-abr-2024
Google ScholarTM
Check
Altmetric
Altmetric
NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.