Matches in UGent Biblio for { <https://biblio.ugent.be/publication/1197972#aggregation> ?p ?o. }
Showing items 1 to 41 of
41
with 100 items per page.
- aggregation classification "A1".
- aggregation creator B217744.
- aggregation creator B217745.
- aggregation creator B217746.
- aggregation creator B217747.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation date "2011".
- aggregation format "application/pdf".
- aggregation hasFormat 1197972.bibtex.
- aggregation hasFormat 1197972.csv.
- aggregation hasFormat 1197972.dc.
- aggregation hasFormat 1197972.didl.
- aggregation hasFormat 1197972.doc.
- aggregation hasFormat 1197972.json.
- aggregation hasFormat 1197972.mets.
- aggregation hasFormat 1197972.mods.
- aggregation hasFormat 1197972.rdf.
- aggregation hasFormat 1197972.ris.
- aggregation hasFormat 1197972.txt.
- aggregation hasFormat 1197972.xls.
- aggregation hasFormat 1197972.yaml.
- aggregation isPartOf urn:issn:1350-9047.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "cIAP1 and TAK1 protect cells from TNF-induced necrosis by preventing RIP1/RIP3-dependent reactive oxygen species production".
- aggregation abstract "Three members of the IAP family (X-linked inhibitor of apoptosis (XIAP), cellular inhibitor of apoptosis proteins-1/-2 (cIAP1 and cIAP2)) are potent suppressors of apoptosis. Recent studies have shown that cIAP1 and cIAP2, unlike XIAP, are not direct caspase inhibitors, but block apoptosis by functioning as E3 ligases for effector caspases and receptor-interacting protein 1 (RIP1). cIAP-mediated polyubiquitination of RIP1 allows it to bind to the pro-survival kinase transforming growth factor-beta-activated kinase 1 (TAK1) which prevents it from activating caspase-8-dependent death, a process reverted by the deubiquitinase CYLD. RIP1 is also a regulator of necrosis, a caspase-independent type of cell death. Here, we show that cells depleted of the IAPs by treatment with the IAP antagonist BV6 are greatly sensitized to tumor necrosis factor (TNF)-induced necrosis, but not to necrotic death induced by anti-Fas, poly(I:C) oxidative stress. Specific targeting of the IAPs by RNAi revealed that repression of cIAP1 is responsible for the sensitization. Similarly, lowering TAK1 levels or inhibiting its kinase activity sensitized cells to TNF-induced necrosis, whereas repressing CYLD had the opposite effect. We show that this sensitization to death is accompanied by enhanced RIP1 kinase activity, increased recruitment of RIP1 to Fas-associated via death domain and RIP3 (which allows necrosome formation), and elevated RIP1 kinase-dependent accumulation of reactive oxygen species (ROS). In conclusion, our data indicate that cIAP1 and TAK1 protect cells from TNF-induced necrosis by preventing RIP1/RIP3-dependent ROS production. Cell Death and Differentiation (2011) 18, 656-665; doi:10.1038/cdd.2010.138; published online 5 November 2010".
- aggregation authorList BK480567.
- aggregation endPage "665".
- aggregation issue "4".
- aggregation startPage "656".
- aggregation volume "18".
- aggregation aggregates 3146953.
- aggregation isDescribedBy 1197972.
- aggregation similarTo cdd.2010.138.
- aggregation similarTo LU-1197972.