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Apolipoprotein L2 contains a BH3-like domain but it does not behave as a BH3-only protein

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dc.contributor.author Galindo-Moreno, Juan
dc.contributor.author Iurlaro, Raffaella
dc.contributor.author El Mjiyad, Nadia
dc.contributor.author Díez-Pérez, Javier
dc.contributor.author Gabaldón Estevan, Juan Antonio, 1973-
dc.contributor.author Muñoz-Pinedo, Cristina
dc.date.accessioned 2023-12-19T07:02:17Z
dc.date.available 2023-12-19T07:02:17Z
dc.date.issued 2014
dc.identifier.citation Galindo-Moreno J, Iurlaro R, El Mjiyad N, Díez-Pérez J, Gabaldón T, Muñoz-Pinedo C. Apolipoprotein L2 contains a BH3-like domain but it does not behave as a BH3-only protein. Cell Death Dis. 2014 Jun 5;5(6):e1275. DOI: 10.1038/cddis.2014.237
dc.identifier.issn 2041-4889
dc.identifier.uri http://hdl.handle.net/10230/58588
dc.description.abstract Apolipoproteins of the L family are lipid-binding proteins whose function is largely unknown. Apolipoprotein L1 and apolipoprotein L6 have been recently described as novel pro-death BH3-only proteins that are also capable of regulating autophagy. In an in-silico screening to discover novel putative BH3-only proteins, we identified yet another member of the apolipoprotein L family, apolipoprotein L2 (ApoL2), as a BH3 motif-containing protein. ApoL2 has been suggested to behave as a BH3-only protein and mediate cell death induced by interferon-gamma or viral infection. As previously described, we observed that ApoL2 protein was induced by interferon-gamma. However, knocking down its expression in HeLa cells did not regulate cell death induced by interferon-gamma. Overexpression of ApoL2 did not induce cell death on its own. ApoL2 did not sensitize or protect cells from overexpression of the BH3-only proteins Bmf or Noxa. Furthermore, siRNA against ApoL2 did not alter sensitivity to a variety of death stimuli. We could, however, detect a weak interaction between ApoL2 and Bcl-2 by immunoprecipitation of the former, suggesting a role of ApoL2 in a Bcl-2-regulated process like autophagy. However, in contrast to what has been described about its homologs ApoL1 and ApoL6, ApoL2 did not regulate autophagy. Thus, the role, if any, of ApoL2 in cell death remains to be clarified.
dc.format.mimetype application/pdf
dc.language.iso eng
dc.publisher Springer
dc.relation.ispartof Cell Death & Disease. 2014 Jun 5;5(6):e1275
dc.rights Cell Death and Disease is an open-access journal published by Nature Publishing Group. This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivs 3.0 Unported License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-nd/3.0/.
dc.rights.uri http://creativecommons.org/licenses/by-nc-nd/3.0/
dc.title Apolipoprotein L2 contains a BH3-like domain but it does not behave as a BH3-only protein
dc.type info:eu-repo/semantics/article
dc.identifier.doi http://dx.doi.org/10.1038/cddis.2014.237
dc.subject.keyword Apolipoproteins L
dc.subject.keyword Bcl-2 family proteins
dc.subject.keyword BH3-only
dc.subject.keyword Interferon-gamma
dc.subject.keyword Autophagy
dc.rights.accessRights info:eu-repo/semantics/openAccess
dc.type.version info:eu-repo/semantics/publishedVersion

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