Access and utilization of long chain fatty acyl-CoA by zDHHC protein acyltransferases |
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| Institution: | 1. Laboratory of Chemical Biology and Microbial Pathogenesis, The Rockefeller University, New York, NY 10065, United States;2. The Crick Institute, 215 Euston Road, London NW1 2BE, United Kingdom;1. Chemical Physics Program, Institute for Physical Sciences and Technology, University of Maryland, College Park, 20742, MD, USA;2. Department of Chemistry and Biochemistry, Center for Biomolecular Structure and Organization, University of Maryland, College Park, 20742, MD, USA;3. Postdoctoral Research Associate Program, National Institute of General Medical Sciences National Institutes of Health (NIH), Bethesda, MD 20892, USA |
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| Abstract: | S-acylation is a reversible posttranslational modification, where a long-chain fatty acid is attached to a protein through a thioester linkage. Being the most abundant form of lipidation in humans, a family of twenty-three human zDHHC integral membrane enzymes catalyze this reaction. Previous structures of the apo and lipid bound zDHHCs shed light into the molecular details of the active site and binding pocket. Here, we delve further into the details of fatty acyl-CoA recognition by zDHHC acyltransferases using insights from the recent structure. We additionally review indirect evidence that suggests acyl-CoAs do not diffuse freely in the cytosol, but are channeled into specific pathways, and comment on the suggested mechanisms for fatty acyl-CoA compartmentalization and intracellular transport, to finally speculate about the potential mechanisms that underlie fatty acyl-CoA delivery to zDHHC enzymes. |
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