Please use this identifier to cite or link to this item: https://hdl.handle.net/10216/116497
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dc.creatorPedrosa, AG-
dc.creatorFrancisco, T-
dc.creatorBicho, D-
dc.creatorDias, AF-
dc.creatorBarros-Barbosa, A-
dc.creatorHagmann, V-
dc.creatorDodt, G-
dc.creatorRodrigues, TA-
dc.creatorAzevedo, JE-
dc.date.accessioned2018-11-12T17:47:25Z-
dc.date.available2018-11-12T17:47:25Z-
dc.date.issued2018-
dc.identifier.issn0021-9258-
dc.identifier.urihttp://hdl.handle.net/10216/116497-
dc.description.abstractPEX1 and PEX6 are two members of the ATPases associated with diverse cellular activities (AAA) family and the core components of the receptor export module of the peroxisomal matrix protein import machinery. Their role is to extract monoubiquitinated PEX5, the peroxisomal protein-shuttling receptor, from the peroxisomal membrane docking/translocation module (DTM), so that a new cycle of protein transportation can start. Recent data have shown that PEX1 and PEX6 form a heterohexameric complex that unfolds substrates by processive threading. However, whether the natural substrate of the PEX1-PEX6 complex is monoubiquitinated PEX5 (Ub-PEX5) itself or some Ub-PEX5-interacting component(s) of the DTM remains unknown. In this work, we used an established cell-free in vitro system coupled with photoaffinity cross-linking and protein PEGylation assays to address this problem. We provide evidence suggesting that DTM-embedded Ub-PEX5 interacts directly with both PEX1 and PEX6 through its ubiquitin moiety and that the PEX5 polypeptide chain is globally unfolded during the ATP-dependent extraction event. These findings strongly suggest that DTM-embedded Ub-PEX5 is a bona fide substrate of the PEX1-PEX6 complex.pt_PT
dc.description.sponsorshipThe authors thank Britta Moellers (Ruhr-Universität Bochum, Germany) for providing plasmids and recombinant protein for the generation of the anti-PEX6 antibody. This work was funded by FEDER (Fundo Europeu de Desenvolvimento Regional), through COMPETE 2020 –Operacional Programme for Competitiveness and Internationalization (POCI), Portugal 2020, and by Portuguese funds through Fundação para a Ciência e Tecnologia (FCT)/Ministério da Ciência, Tecnologia e Inovação in the framework of the projects “Institute for Research and Innovation in Health Sciences” (POCI-01-0145-FEDER-007274) and “The molecular mechanisms of peroxisome biogenesis” (PTDC/BEX-BCM/2311/2014), and through Norte 2020 – Programa Operacional Regional do Norte, under the application of the “Porto Neurosciences and Neurologic Disease Research Initiative at i3S” (NORTE-01-0145-FEDER-000008). A.G.P, T.F., D.B., A.F.D., A.B.B. and T.A.R. are supported by Fundação para a Ciência e Tecnologia, Programa Operacional Potencial Humano do QREN and Fundo Social Europeu.pt_PT
dc.language.isoengpt_PT
dc.publisherAmerican Society for Biochemistry and Molecular Biologypt_PT
dc.relation.ispartofseriesThe Journal of biological chemistry, vol. 293(29), p. 11553-11563pt_PT
dc.rightsopenAccesspt_PT
dc.subjectATPases associated with diverse cellular activities (AAA)pt_PT
dc.subjectPEX1pt_PT
dc.subjectPEX5pt_PT
dc.subjectPEX6pt_PT
dc.subjectPeroxisomept_PT
dc.subjectProtein sortingpt_PT
dc.subjectProtein translocationpt_PT
dc.subjectUbiquitinpt_PT
dc.titlePeroxisomal monoubiquitinated PEX5 interacts with the AAA ATPases PEX1 and PEX6 and is unfolded during its dislocation into the cytosolpt_PT
dc.typeArtigo em Revista Científica Internacionalpt_PT
dc.contributor.uportoInstituto de Investigação e Inovação em Saúdept_PT
dc.identifier.doi10.1074/jbc.RA118.003669-
dc.relation.publisherversionhttp://www.jbc.org/content/293/29/11553.long-
Appears in Collections:I3S - Artigo em Revista Científica Internacional

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