The diversity of ACBD proteins – From lipid binding to protein modulators and organelle tethers
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 cellu...
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Published in | Biochimica et biophysica acta. Molecular cell research Vol. 1867; no. 5; p. 118675 |
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Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
Published |
Netherlands
Elsevier B.V
01.05.2020
Elsevier |
Subjects | |
Online Access | Get full text |
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Summary: | 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.
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•Acyl-CoA binding domain-containing proteins (ACBDs) can be found among eukaryotes and prokaryotes.•Additional protein interaction domains are a characteristic of most extended ACBDs.•A set of a small ACBD and an ACBD with a C-terminal ankyrin-repeat motif is found in all eukaryote branches.•Fungi and metazoans contain genes for ACBD5/ATG37 but the proteins do not appear to possess conserved functions•Several extended metazoan ACBDs are hijacked by viruses in order to facilitate effective viral replication. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-3 content type line 23 ObjectType-Review-1 |
ISSN: | 0167-4889 1879-2596 |
DOI: | 10.1016/j.bbamcr.2020.118675 |