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The diversity of ACBD proteins - From lipid binding to protein modulators and organelle tethers

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ELSEVIER
DOI: 10.1016/j.bbamcr.2020.118675

关键词

Acyl-CoA binding domain containing protein; Peroxisomes; Lipid metabolism; Membrane contact sites; FFAT motif; Pathogen host interaction

资金

  1. Biotechnology and Biological Sciences Research Council (BBSRC) [BB/N01541X/1, BB/T002255/1]
  2. Medical Research Council (MRC) [CiC 08135]
  3. University of Exeter
  4. European Union [812968 PERICO]
  5. German Research Foundation (DFG) [397476530]
  6. GW4 BioMed MRC Doctoral Training Partnership [MR/N0137941/1]
  7. BBSRC [BB/T002255/1, BB/N01541X/1, BB/M011801/1] Funding Source: UKRI
  8. MRC [2073760] Funding Source: UKRI

向作者/读者索取更多资源

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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