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The C-terminal domains of apoptotic BH3-only proteins mediate their insertion into distinct biological membranes

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The C-terminal domains of apoptotic BH3-only proteins mediate their insertion into distinct biological membranes

dc.contributor.author	Andreu Fernández, Vicente
dc.contributor.author	García Murria, María Jesús
dc.contributor.author	Bañó Polo, Manuel
dc.contributor.author	Martin, Juliette
dc.contributor.author	Monticelli, Luca
dc.contributor.author	Orzáez Calatayud, María del Mar
dc.contributor.author	Mingarro Muñoz, Ismael
dc.date.accessioned	2016-12-07T15:11:08Z
dc.date.available	2016-12-07T15:11:08Z
dc.date.issued	2016
dc.identifier.citation	Andreu Fernández, Vicente García Murria, María Jesús Bañó Polo, Manuel Martin, Juliette Monticelli, Luca Orzáez Calatayud, María del Mar Mingarro Muñoz, Ismael 2016 The C-terminal domains of apoptotic BH3-only proteins mediate their insertion into distinct biological membranes Journal of Biological Chemistry 291 48 25207 25216
dc.identifier.uri	http://hdl.handle.net/10550/56287
dc.description.abstract	Changes in the equilibrium of pro- and anti-apoptotic members of the B-cell lymphoma-2 (Bcl-2) protein family in the mitochondrial outer membrane (MOM) induce structural changes that commit cells to apoptosis. Bcl-2 homology-3 (BH3)-only proteins participate in this process by either activating pro-apoptotic effectors or inhibiting anti-apoptotic components and by promoting MOM permeabilization. The association of BH3-only proteins with MOMs is necessary for the activation and amplification of death signals; however, the nature of this association remains controversial, as these proteins lack a canonical transmembrane sequence. Here we used an in vitro expression system to study the insertion capacity of hydrophobic C-terminal regions of the BH3-only proteins Bik, Bim, Noxa, Bmf, and Puma into microsomal membranes. An Escherichia coli complementation assay was used to validate the results in a cellular context, and peptide insertions were modeled using molecular dynamics simulations. We also found that some of the C-terminal domains were sufficient to direct green fluorescent protein-fusion proteins to specific membranes in human cells, but the domains did not activate apoptosis. Thus, the hydrophobic regions in the C-termini of BH3-only members associated in distinct ways with various biological membranes, suggesting that a detailed investigation of the entire process of apoptosis should include studying the membranes as a setting for protein-protein and protein-membrane interactions.
dc.language.iso	eng
dc.relation.ispartof	Journal of Biological Chemistry, 2016, vol. 291, num. 48, p. 25207-25216
dc.subject	Cèl·lules
dc.subject	Proteïnes de membrana
dc.subject	Membranes (Biologia)
dc.title	The C-terminal domains of apoptotic BH3-only proteins mediate their insertion into distinct biological membranes
dc.type	journal article	es_ES
dc.date.updated	2016-12-07T15:11:08Z
dc.identifier.doi	10.1074/jbc.M116.733634
dc.identifier.idgrec	114197
dc.rights.accessRights	open access	es_ES