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dc.contributor.authorRodríguez-Galán, Olgaes_ES
dc.contributor.authorGalindo, Antonioes_ES
dc.contributor.authorHervás-Aguilar, Américaes_ES
dc.contributor.authorArst, Herbert Nathan Jr.es_ES
dc.contributor.authorPeñalva, Miguel Ángeles_ES
dc.date.accessioned2018-01-05T12:47:42Z-
dc.date.available2018-01-05T12:47:42Z-
dc.date.issued2009-02-13-
dc.identifier.citationJ Biol Chem. 284(7):4404-12 (2009)es_ES
dc.identifier.issn0021-9258-
dc.identifier.urihttp://hdl.handle.net/10261/158866-
dc.description10 p.-5 figes_ES
dc.description.abstractActivation of the Aspergillus nidulans transcription factor PacC, which mediates ambient pH regulation of gene expression and is recruited to ESCRT-III by the Vps32-interacting scaffold PalA, involves its ambient pH-dependent C-terminal proteolysis. This reaction is almost certainly catalyzed by the PalB calpain-like protease. Here we show that PalB associates with membranes and interacts specifically and directly with ESCRT-III Vps24. The PalB N-terminal MIT domain and the Vps24 C-terminal MIM motif are necessary and sufficient for this interaction. PalB(DeltaMIT), a mutant PalB lacking the MIT domain is inefficiently recruited to membranes and impaired in PacC proteolytic processing. Notably, membrane recruitment is promoted and PacC processing largely restored by covalent attachment of Vps24 to mutant PalB(DeltaMIT). This is the first reported evidence that calpain-like recruitment to ESCRT-III lattices plays a physiological role. It unambiguously positions the calpain-like protease PalB within the ESCRT-III-associated pH signaling complex, underlines the positive role of ESCRT-III in ambient pH signal transduction, and suggests a possible mechanism for PalB activation.es_ES
dc.language.isoenges_ES
dc.publisherAmerican Society for Biochemistry and Molecular Biologyes_ES
dc.relation.isversionofPublisher's versiones_ES
dc.rightsopenAccesses_ES
dc.titlePhysiological involvement in pH signaling of Vps24-mediated recruitment of Aspergillus PalB cysteine protease to ESCRT-III*es_ES
dc.typeArtículoes_ES
dc.identifier.doi10.1074/jbc.M808645200-
dc.description.peerreviewedPeer reviewedes_ES
dc.relation.publisherversionhttp://dx.doi.org/10.1074/jbc.M808645200es_ES
dc.identifier.e-issn1083-351X-
dc.relation.csices_ES
oprm.item.hasRevisionno ko 0 false*
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