dc.contributor.author | Bonekamp, NA | |
dc.contributor.author | Grille, S | |
dc.contributor.author | Cardoso, MJ | |
dc.contributor.author | Almeida, M | |
dc.contributor.author | Aroso, M | |
dc.contributor.author | Gomes, Silvia | |
dc.contributor.author | Magalhaes, AC | |
dc.contributor.author | Ribeiro, D | |
dc.contributor.author | Islinger, M | |
dc.contributor.author | Schrader, M | |
dc.date.accessioned | 2015-06-23T08:54:44Z | |
dc.date.issued | 2013-01-07 | |
dc.description.abstract | Pex11 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.sponsorship | Portuguese Foundation for Science and Technology (FCT) | en_GB |
dc.description.sponsorship | FEDER | en_GB |
dc.description.sponsorship | CRUP/DAAD | en_GB |
dc.identifier.citation | Vol. 8, Iss. 1, pp. e53424 | en_GB |
dc.identifier.doi | 10.1371/journal.pone.0053424 | |
dc.identifier.grantnumber | PTDC/BIA-BCM/099613/2008 | en_GB |
dc.identifier.grantnumber | SFRH/BD/37647/2007 | en_GB |
dc.identifier.grantnumber | SFRH/BD/45427/2008 | en_GB |
dc.identifier.grantnumber | SFRH/BD/80542/2011 | en_GB |
dc.identifier.grantnumber | SFRH/BD/48722/2008 | en_GB |
dc.identifier.grantnumber | SFRH/BD/81223/2011 | en_GB |
dc.identifier.grantnumber | SFRH/BPD/77619/2011 | en_GB |
dc.identifier.grantnumber | SFRH/BPD/74428/2010 | en_GB |
dc.identifier.grantnumber | ACÇÕES INTEGRADAS 2010, A-29/11 | en_GB |
dc.identifier.other | PONE-D-12-25944 | |
dc.identifier.uri | http://hdl.handle.net/10871/17648 | |
dc.language.iso | en | en_GB |
dc.publisher | Public Library of Science | en_GB |
dc.relation.url | http://www.ncbi.nlm.nih.gov/pubmed/23308220 | en_GB |
dc.relation.url | http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0053424 | en_GB |
dc.rights | This 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.subject | Animals | en_GB |
dc.subject | COS Cells | en_GB |
dc.subject | Cercopithecus aethiops | en_GB |
dc.subject | Humans | en_GB |
dc.subject | Intracellular Membranes | en_GB |
dc.subject | Membrane Proteins | en_GB |
dc.subject | Peroxisomes | en_GB |
dc.subject | Phosphorylation | en_GB |
dc.subject | Protein Interaction Domains and Motifs | en_GB |
dc.subject | Protein Structure, Secondary | en_GB |
dc.subject | Recombinant Fusion Proteins | en_GB |
dc.subject | Transfection | en_GB |
dc.title | Self-interaction of human Pex11pβ during peroxisomal growth and division. | en_GB |
dc.type | Article | en_GB |
dc.date.available | 2015-06-23T08:54:44Z | |
dc.identifier.issn | 1932-6203 | |
exeter.place-of-publication | United States | |
dc.description | Journal Article | en_GB |
dc.description | Research Support, Non-U.S. Gov't | en_GB |
dc.description | Copyright: © 2013 Bonekamp et al. | en_GB |
dc.identifier.journal | PLoS One | en_GB |