Show simple item record

dc.contributor.authorBonekamp, NA
dc.contributor.authorGrille, S
dc.contributor.authorCardoso, MJ
dc.contributor.authorAlmeida, M
dc.contributor.authorAroso, M
dc.contributor.authorGomes, Silvia
dc.contributor.authorMagalhaes, AC
dc.contributor.authorRibeiro, D
dc.contributor.authorIslinger, M
dc.contributor.authorSchrader, M
dc.date.accessioned2015-06-23T08:54:44Z
dc.date.issued2013-01-07
dc.description.abstractPex11 proteins are involved in membrane elongation and division processes associated with the multiplication of peroxisomes. Human Pex11pβ has recently been linked to a new disorder affecting peroxisome morphology and dynamics. Here, we have analyzed the exact membrane topology of Pex11pβ. Studies with an epitope-specific antibody and protease protection assays show that Pex11pβ is an integral membrane protein with two transmembrane domains flanking an internal region exposed to the peroxisomal matrix and N- and C-termini facing the cytosol. A glycine-rich internal region within Pex11pβ is dispensable for peroxisome membrane elongation and division. However, we demonstrate that an amphipathic helix (Helix 2) within the first N-terminal 40 amino acids is crucial for membrane elongation and self-interaction of Pex11pβ. Interestingly, we find that Pex11pβ self-interaction strongly depends on the detergent used for solubilization. We also show that N-terminal cysteines are not essential for membrane elongation, and that putative N-terminal phosphorylation sites are dispensable for Pex11pβ function. We propose that self-interaction of Pex11pβ regulates its membrane deforming activity in conjunction with membrane lipids.en_GB
dc.description.sponsorshipPortuguese Foundation for Science and Technology (FCT)en_GB
dc.description.sponsorshipFEDERen_GB
dc.description.sponsorshipCRUP/DAADen_GB
dc.identifier.citationVol. 8, Iss. 1, pp. e53424en_GB
dc.identifier.doi10.1371/journal.pone.0053424
dc.identifier.grantnumberPTDC/BIA-BCM/099613/2008en_GB
dc.identifier.grantnumberSFRH/BD/37647/2007en_GB
dc.identifier.grantnumberSFRH/BD/45427/2008en_GB
dc.identifier.grantnumberSFRH/BD/80542/2011en_GB
dc.identifier.grantnumberSFRH/BD/48722/2008en_GB
dc.identifier.grantnumberSFRH/BD/81223/2011en_GB
dc.identifier.grantnumberSFRH/BPD/77619/2011en_GB
dc.identifier.grantnumberSFRH/BPD/74428/2010en_GB
dc.identifier.grantnumberACÇÕES INTEGRADAS 2010, A-29/11en_GB
dc.identifier.otherPONE-D-12-25944
dc.identifier.urihttp://hdl.handle.net/10871/17648
dc.language.isoenen_GB
dc.publisherPublic Library of Scienceen_GB
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pubmed/23308220en_GB
dc.relation.urlhttp://journals.plos.org/plosone/article?id=10.1371/journal.pone.0053424en_GB
dc.rightsThis is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.en_GB
dc.subjectAnimalsen_GB
dc.subjectCOS Cellsen_GB
dc.subjectCercopithecus aethiopsen_GB
dc.subjectHumansen_GB
dc.subjectIntracellular Membranesen_GB
dc.subjectMembrane Proteinsen_GB
dc.subjectPeroxisomesen_GB
dc.subjectPhosphorylationen_GB
dc.subjectProtein Interaction Domains and Motifsen_GB
dc.subjectProtein Structure, Secondaryen_GB
dc.subjectRecombinant Fusion Proteinsen_GB
dc.subjectTransfectionen_GB
dc.titleSelf-interaction of human Pex11pβ during peroxisomal growth and division.en_GB
dc.typeArticleen_GB
dc.date.available2015-06-23T08:54:44Z
dc.identifier.issn1932-6203
exeter.place-of-publicationUnited States
dc.descriptionJournal Articleen_GB
dc.descriptionResearch Support, Non-U.S. Gov'ten_GB
dc.descriptionCopyright: © 2013 Bonekamp et al.en_GB
dc.identifier.journalPLoS Oneen_GB


Files in this item

This item appears in the following Collection(s)

Show simple item record