{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Rosa N"],"funding":["Onderzoeksraad, KU Leuven","NIDCR NIH HHS","U.S. Department of Health &amp; Human Services | NIH | National Institute of Dental and Craniofacial Research","Federaal Wetenschapsbeleid","Fonds Wetenschappelijk Onderzoek","Central European Leuven Strategic Alliance - CELSA/18/040","Gouvernement du Canada | Canadian Institutes of Health Research","CIHR"],"pagination":["788-805"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8990011"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["29(4)"],"pubmed_abstract":["Anti-apoptotic Bcl-2-family members not only act at mitochondria but also at the endoplasmic reticulum, where they impact Ca<sup>2+</sup> dynamics by controlling IP<sub>3</sub> receptor (IP<sub>3</sub>R) function. Current models propose distinct roles for Bcl-2 vs. Bcl-xL, with Bcl-2 inhibiting IP<sub>3</sub>Rs and preventing pro-apoptotic Ca<sup>2+</sup> release and Bcl-xL sensitizing IP<sub>3</sub>Rs to low [IP<sub>3</sub>] and promoting pro-survival Ca<sup>2+</sup> oscillations. We here demonstrate that Bcl-xL too inhibits IP<sub>3</sub>R-mediated Ca<sup>2+</sup> release by interacting with the same IP<sub>3</sub>R regions as Bcl-2. Via in silico superposition, we previously found that the residue K87 of Bcl-xL spatially resembled K17 of Bcl-2, a residue critical for Bcl-2's IP<sub>3</s"],"journal":["Cell death and differentiation"],"pubmed_title":["Bcl-xL acts as an inhibitor of IP<sub>3</sub>R channels, thereby antagonizing Ca<sup>2+</sup>-driven apoptosis."],"pmcid":["PMC8990011"],"funding_grant_id":["G0H1716N","R01 DE014756","FDN143312","AKUL/19/34","R56 DE014756","AKUL/15/34","OT14/101","DE014756","C14/19/099","IAP-P7/13","G.0901.18N","W0.019.17N","12P0919N","C14/19/101"],"pubmed_authors":["Karamanou S","Yule DI","Bultynck G","Hamada K","Schymkowitz J","Rousseau F","Rosa N","La Rovere R","Lemmens I","Vandermarliere E","Ando H","Andrews DW","Shabardina V","Economou A","Wagner LE","Welkenhuyzen K","Ivanova H","Tavernier J","Louros N","Kale J","Parys JB","Mikoshiba K"],"additional_accession":[]},"is_claimable":false,"name":"Bcl-xL acts as an inhibitor of IP<sub>3</sub>R channels, thereby antagonizing Ca<sup>2+</sup>-driven apoptosis.","description":"Anti-apoptotic Bcl-2-family members not only act at mitochondria but also at the endoplasmic reticulum, where they impact Ca<sup>2+</sup> dynamics by controlling IP<sub>3</sub> receptor (IP<sub>3</sub>R) function. Current models propose distinct roles for Bcl-2 vs. Bcl-xL, with Bcl-2 inhibiting IP<sub>3</sub>Rs and preventing pro-apoptotic Ca<sup>2+</sup> release and Bcl-xL sensitizing IP<sub>3</sub>Rs to low [IP<sub>3</sub>] and promoting pro-survival Ca<sup>2+</sup> oscillations. We here demonstrate that Bcl-xL too inhibits IP<sub>3</sub>R-mediated Ca<sup>2+</sup> release by interacting with the same IP<sub>3</sub>R regions as Bcl-2. Via in silico superposition, we previously found that the residue K87 of Bcl-xL spatially resembled K17 of Bcl-2, a residue critical for Bcl-2's IP<sub>3</s","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Apr","modification":"2025-04-04T08:24:03.239Z","creation":"2025-04-04T08:24:03.239Z"},"accession":"S-EPMC8990011","cross_references":{"pubmed":["34750538"],"doi":["10.1038/s41418-021-00894-w"]}}