dc.contributor.author | Costello, J | |
dc.contributor.author | Castro, I | |
dc.contributor.author | Schrader, TA | |
dc.contributor.author | Islinger, M | |
dc.contributor.author | Schrader, M | |
dc.date.accessioned | 2017-03-31T09:15:08Z | |
dc.date.issued | 2017-05-02 | |
dc.description.abstract | Cooperation between cellular organelles such as mitochondria, peroxisomes and the ER is
essential for a variety of important and diverse metabolic processes. Effective communication
and metabolite exchange requires physical linkages between the organelles, predominantly in
the form of organelle contact sites. At such contact sites organelle membranes are brought
into close proximity by the action of molecular tethers, which often consist of specific protein
pairs anchored in the membrane of the opposing organelles. Currently numerous tethering
components have been identified which link the ER with multiple other organelles but
knowledge of the factors linking the ER with peroxisomes is limited. Peroxisome-ER
interplay is important because it is required for the biosynthesis of unsaturated fatty acids,
ether-phospholipids and sterols with defects in these functions leading to severe diseases.
Here we characterise acyl-CoA binding domain protein 4 (ACBD4) as a tail-anchored
peroxisomal membrane protein which interacts with the ER protein, vesicle-associated
membrane protein-associated protein–B (VAPB) to promote peroxisome-ER associations. | en_GB |
dc.description.sponsorship | We thank all colleagues who provided plasmids and antibodies, and T Levine for sharing
data. This work was supported by BBSRC (BB/K006231/1, BB/N01541X/1). MS is
supported by the Marie Curie Initial Training Network action PerFuMe (316723). The
authors declare no competing financial interests. | en_GB |
dc.identifier.citation | Published online: 02 May 2017 | en_GB |
dc.identifier.doi | http://dx.doi.org/10.1080/15384101.2017.1314422 | |
dc.identifier.uri | http://hdl.handle.net/10871/26878 | |
dc.language.iso | en | en_GB |
dc.publisher | Taylor & Francis | en_GB |
dc.rights | © 2017 The Author(s). Published with license by Taylor & Francis© Joseph L. Costello, Inês G. Castro, Tina A. Schrader, Markus Islinger, and Michael Schrader
This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted. | |
dc.subject | Peroxisomes | en_GB |
dc.subject | ER | en_GB |
dc.subject | ACBD4 | en_GB |
dc.subject | VAPB | en_GB |
dc.subject | membrane contact sites | en_GB |
dc.title | Peroxisomal ACBD4 interacts with VAPB and promotes ER-peroxisome associations | en_GB |
dc.type | Article | en_GB |
dc.identifier.issn | 1538-4101 | |
dc.description | This is the author accepted manuscript. The final version is available from Taylor & Francis via the DOI in this record. | |
dc.identifier.eissn | 1551-4005 | |
dc.identifier.journal | Cell Cycle | en_GB |