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Bax transmembrane domain interacts with prosurvival Bcl-2 proteins in biological membranes

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Bax transmembrane domain interacts with prosurvival Bcl-2 proteins in biological membranes

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dc.contributor.author Andreu Fernández,Vicente
dc.contributor.author Sancho, Mónica
dc.contributor.author Genovés, Ainhoa
dc.contributor.author Lucendo, Estefanía
dc.contributor.author Todt, Franziska
dc.contributor.author Lauterwasser, Joachim
dc.contributor.author Funk, Kathrin
dc.contributor.author Jahreis, Günther
dc.contributor.author Pérez Payá, Enrique
dc.contributor.author Mingarro Muñoz, Ismael
dc.contributor.author Edlich, Frank
dc.contributor.author Orzáez Calatayud, María del Mar
dc.date.accessioned 2019-11-12T12:02:02Z
dc.date.available 2019-11-12T12:02:02Z
dc.date.issued 2017
dc.identifier.citation Andreu Fernández,Vicente Sancho, Mónica Genovés, Ainhoa Lucendo, Estefanía Todt, Franziska Lauterwasser, Joachim Funk, Kathrin Jahreis, Günther Pérez Payá, Enrique Mingarro Muñoz, Ismael Edlich, Frank Orzáez Calatayud, María del Mar 2017 Bax transmembrane domain interacts with prosurvival Bcl-2 proteins in biological membranes Proceedings of the National Academy of Sciences of the United States of America 114 2 310 315
dc.identifier.uri https://hdl.handle.net/10550/72177
dc.description.abstract The Bcl-2 (B-cell lymphoma 2) protein Bax (Bcl-2 associated X, apoptosis regulator) can commit cells to apoptosis via outer mitochondrial membrane permeabilization. Bax activity is controlled in healthy cells by prosurvival Bcl-2 proteins. C-terminal Bax transmembrane domain interactions were implicated recently in Bax pore formation. Here, we show that the isolated transmembrane domains of Bax, Bcl-xL (B-cell lymphoma-extra large), and Bcl-2 can mediate interactions between Bax and prosurvival proteins inside the membrane in the absence of apoptotic stimuli. Bcl-2 protein transmembrane domains specifically homooligomerize and heterooligomerize in bacterial and mitochondrial membranes. Their interactions participate in the regulation of Bcl-2 proteins, thus modulating apoptotic activity. Our results suggest that interactions between the transmembrane domains of Bax and antiapoptotic Bcl-2 proteins represent a previously unappreciated level of apoptosis regulation.
dc.language.iso eng
dc.relation.ispartof Proceedings of the National Academy of Sciences of the United States of America, 2017, vol. 114, num. 2, p. 310-315
dc.subject Biotecnologia
dc.subject Proteïnes
dc.subject Membranes (Biologia)
dc.title Bax transmembrane domain interacts with prosurvival Bcl-2 proteins in biological membranes
dc.type journal article es_ES
dc.date.updated 2019-11-12T12:02:03Z
dc.identifier.doi 10.1073/pnas.1612322114
dc.identifier.idgrec 116625
dc.rights.accessRights open access es_ES

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