Matches in UGent Biblio for { <https://biblio.ugent.be/publication/2106375#aggregation> ?p ?o. }
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- aggregation classification "A1".
- aggregation creator B293684.
- aggregation creator B293685.
- aggregation creator B293686.
- aggregation creator B293687.
- aggregation creator B293688.
- aggregation creator B293689.
- aggregation creator B293690.
- aggregation creator B293691.
- aggregation creator B293692.
- aggregation creator B293693.
- aggregation creator B293694.
- aggregation creator person.
- aggregation creator person.
- aggregation date "2012".
- aggregation format "application/pdf".
- aggregation hasFormat 2106375.bibtex.
- aggregation hasFormat 2106375.csv.
- aggregation hasFormat 2106375.dc.
- aggregation hasFormat 2106375.didl.
- aggregation hasFormat 2106375.doc.
- aggregation hasFormat 2106375.json.
- aggregation hasFormat 2106375.mets.
- aggregation hasFormat 2106375.mods.
- aggregation hasFormat 2106375.rdf.
- aggregation hasFormat 2106375.ris.
- aggregation hasFormat 2106375.txt.
- aggregation hasFormat 2106375.xls.
- aggregation hasFormat 2106375.yaml.
- aggregation isPartOf urn:issn:1350-9047.
- aggregation language "eng".
- aggregation rights "I have retained and own the full copyright for this publication".
- aggregation subject "Biology and Life Sciences".
- aggregation title "Selective regulation of IP3-receptor-mediated Ca2+ signaling and apoptosis by the BH4 domain of Bcl-2 versus Bcl-Xl".
- aggregation abstract "Antiapoptotic B-cell lymphoma 2 (Bcl-2) targets the inositol 1,4,5-trisphosphate receptor (IP3R) via its BH4 domain, thereby suppressing IP3R Ca2+-flux properties and protecting against Ca2+-dependent apoptosis. Here, we directly compared IP3R inhibition by BH4-Bcl-2 and BH4-Bcl-Xl. In contrast to BH4-Bcl-2, BH4-Bcl-Xl neither bound the modulatory domain of IP3R nor inhibited IP3-induced Ca2+ release (IICR) in permeabilized and intact cells. We identified a critical residue in BH4-Bcl-2 (Lys17) not conserved in BH4-Bcl-Xl (Asp11). Changing Lys17 into Asp in BH4-Bcl-2 completely abolished its IP3R-binding and -inhibitory properties, whereas changing Asp11 into Lys in BH4-Bcl-Xl induced IP3R binding and inhibition. This difference in IP3R regulation between BH4-Bcl-2 and BH4-Bcl-Xl controls their antiapoptotic action. Although both BH4-Bcl-2 and BH4-Bcl-Xl had antiapoptotic activity, BH4-Bcl-2 was more potent than BH4-Bcl-Xl. The effect of BH4-Bcl-2, but not of BH4-Bcl-Xl, depended on its binding to IP(3)Rs. In agreement with the IP3R-binding properties, the antiapoptotic activity of BH4-Bcl-2 and BH4-Bcl-Xl was modulated by the Lys/Asp substitutions. Changing Lys17 into Asp in full-length Bcl-2 significantly decreased its binding to the IP3R, its ability to inhibit IICR and its protection against apoptotic stimuli. A single amino-acid difference between BH4-Bcl-2 and BH4-Bcl-Xl therefore underlies differential regulation of IP(3)Rs and Ca2+-driven apoptosis by these functional domains. Mutating this residue affects the function of Bcl-2 in Ca2+ signaling and apoptosis.".
- aggregation authorList BK579563.
- aggregation endPage "309".
- aggregation issue "2".
- aggregation startPage "295".
- aggregation volume "19".
- aggregation aggregates 2106580.
- aggregation isDescribedBy 2106375.
- aggregation similarTo cdd.2011.97.
- aggregation similarTo LU-2106375.