Islinger, M;
Costello, JL;
Kors, S;
Soupene, E;
Levine, TP;
Kuypers, FA;
Schrader, M;
(2020)
The diversity of ACBD proteins - From lipid binding to protein modulators and organelle tethers.
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
, 1867
(5)
, Article 118675. 10.1016/j.bbamcr.2020.118675.
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Abstract
Members of the large multigene family of acyl-CoA binding domain containing proteins (ACBDs) share a conserved motif required for binding of Coenzyme A esterified fatty acids of various chain length. These proteins are present in the three kingdoms of life, and despite their predicted roles in cellular lipid metabolism, knowledge about the precise functions of many ACBD proteins remains scarce. Interestingly, several ACBD proteins are now suggested to function at organelle contact sites, and are recognized as host interaction proteins for different pathogens including viruses and bacteria. Here, we present a thorough phylogenetic analysis of the ACBD family and discuss their structure and evolution. We summarize recent findings on the various functions of animal and fungal ACBDs with particular focus on peroxisomes, the role of ACBD proteins at organelle membranes, and their increasing recognition as targets for pathogens.
| Type: | Article |
|---|---|
| Title: | The diversity of ACBD proteins - From lipid binding to protein modulators and organelle tethers |
| Location: | Netherlands |
| Open access status: | An open access version is available from UCL Discovery |
| DOI: | 10.1016/j.bbamcr.2020.118675 |
| Publisher version: | https://doi.org/10.1016/j.bbamcr.2020.118675 |
| Language: | English |
| Additional information: | This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
| Keywords: | Acyl-CoA binding domain containing protein, FFAT motif, Lipid metabolism, Membrane contact sites, Pathogen host interaction, Peroxisomes |
| UCL classification: | UCL UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Brain Sciences > Institute of Ophthalmology |
| URI: | https://discovery.ucl.ac.uk/id/eprint/10092144 |
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