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

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

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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.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.rights.uri info:eu-repo/semantics/openAccess
dc.source 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.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 info:eu-repo/semantics/article
dc.date.updated 2016-12-07T15:11:08Z
dc.identifier.doi http://dx.doi.org/10.1074/jbc.M116.733634
dc.identifier.idgrec 114197

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