Journal article : Review
Post-translational palmitoylation of metabolic proteins
- Abstract:
- Numerous cellular proteins are post-translationally modified by addition of a lipid group to their structure, which dynamically influences the proteome by increasing hydrophobicity of proteins often impacting protein conformation, localization, stability, and binding affinity. These lipid modifications include myristoylation and palmitoylation. Palmitoylation involves a 16-carbon saturated fatty acyl chain being covalently linked to a cysteine thiol through a thioester bond. Palmitoylation is unique within this group of modifications, as the addition of the palmitoyl group is reversible and enzyme driven, rapidly affecting protein targeting, stability and subcellular trafficking. The palmitoylation reaction is catalyzed by a large family of Asp-His-His-Cys (DHHCs) motif-containing palmitoyl acyltransferases, while the reverse reaction is catalyzed by acyl-protein thioesterases (APTs), that remove the acyl chain. Palmitoyl-CoA serves an important dual purpose as it is not only a key metabolite fueling energy metabolism, but is also a substrate for this PTM. In this review, we discuss protein palmitoylation in regulating substrate metabolism, focusing on membrane transport proteins and kinases that participate in substrate uptake into the cell. We then explore the palmitoylation of mitochondrial proteins and the palmitoylation regulatory enzymes, a less explored field for potential lipid metabolic regulation.
- Publication status:
- Published
- Peer review status:
- Peer reviewed
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(Preview, Version of record, pdf, 1.3MB, Terms of use)
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- Publisher copy:
- 10.3389/fphys.2023.1122895
Authors
- Publisher:
- Frontiers Media
- Journal:
- Frontiers in physiology More from this journal
- Volume:
- 14
- Article number:
- 1122895
- Place of publication:
- Switzerland
- Publication date:
- 2023-02-24
- Acceptance date:
- 2023-02-03
- DOI:
- EISSN:
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1664-042X
- ISSN:
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1664-042X
- Pmid:
-
36909239
- Language:
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English
- Keywords:
- Subtype:
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Review
- Pubs id:
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1333043
- Local pid:
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pubs:1333043
- Deposit date:
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2023-07-04
- ARK identifier:
Terms of use
- Copyright holder:
- Dennis and Heather
- Copyright date:
- 2023
- Rights statement:
- © 2023 Dennis and Heather. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
- Licence:
- CC Attribution (CC BY)
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