ArticleProceedings of the National Academy of Sciences of the United States of America2022
Bivalent recognition of fatty acyl-CoA by a human integral membrane palmitoyltransferase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 30 citations in OpenAlex.
- Druggable β-catenin palmitoyl-switch coordinates immune evasion via immunogenic ferroptosis resistance and PD-L1-mediated immunosuppression.Cell reports. Medicine · 2026Article
- Screening of ester-forming and hydrolyzing enzymes linked to pheromone production in Ips typographus (Linnaeus, 1758).BMC genomics · 2026Article
- ZDHHC-Mediated Protein S-Palmitoylation in Cancer: Epigenetic Interfaces, Structural Logic and Therapeutic Targeting.International journal of medical sciences · 2026Review
- Protein S-Palmitoylation as Potential Therapeutic Target for Dermatoses.Biomolecules · 2025Review
- Lipid overload meets S-palmitoylation: a metabolic signalling nexus driving cardiovascular and heart disease.Cell communication and signaling : CCS · 2025Review
- Greasing the wheels of inflammasome formation: regulation of NLRP3 function by S-linked fatty acids.Biochemical Society transactions · 2025Article
- Protein palmitoylation: an emerging regulator of inflammatory signaling and diseases.Frontiers in immunology · 2025Review
- Predicting protein interactions of the kinase Lck critical to T cell modulation.Structure (London, England : 1993) · 2024Article
- A palmitoyl transferase chemical-genetic system to map ZDHHC-specific S-acylation.Nature biotechnology · 2024Article
- zDHHC20-driven S-palmitoylation of CD80 is required for its costimulatory function.Acta pharmacologica Sinica · 2024Article
- Mechanisms and functions of protein S-acylation.Nature reviews. Molecular cell biology · 2024Review
- Protein lipidation in cancer: mechanisms, dysregulation and emerging drug targets.Nature reviews. Cancer · 2024Review
- Regulation of RAS palmitoyltransferases by accessory proteins and palmitoylation.Nature structural & molecular biology · 2024Article
- Research progress on S-palmitoylation modification mediated by the ZDHHC family in glioblastoma.Frontiers in cell and developmental biology · 2024Review
- The role of an amphiphilic helix and transmembrane region in the efficient acylation of the M2 protein from influenza virus.Scientific reports · 2023Article
- The role of s-palmitoylation in neurological diseases: implication for zDHHC family.Frontiers in pharmacology · 2023Review
- Access and utilization of long chain fatty acyl-CoA by zDHHC protein acyltransferases.Current opinion in structural biology · 2022Review
- The Mechanism of Selective Recognition of Lipid Substrate by hDHHC20 Enzyme.International journal of molecular sciences · 2022Article
- Charting the Chemical Space of Acrylamide-Based Inhibitors of zDHHC20.ACS medicinal chemistry letters · 2022Article
- A High-Throughput Fluorescent Turn-On Assay for Inhibitors of DHHC Family Proteins.ACS chemical biology · 2022Article
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
Abstract
S-acylation, also known as palmitoylation, is the most abundant form of protein lipidation in humans. This reversible posttranslational modification, which targets thousands of proteins, is catalyzed by 23 members of the DHHC family of integral membrane enzymes. DHHC enzymes use fatty acyl-CoA as the ubiquitous fatty acyl donor and become autoacylated at a catalytic cysteine; this intermediate subsequently transfers the fatty acyl group to a cysteine in the target protein. Protein S-acylation intersects with almost all areas of human physiology, and several DHHC enzymes are considered as possible therapeutic targets against diseases such as cancer. These efforts would greatly benefit from a detailed understanding of the molecular basis for this crucial enzymatic reaction. Here, we combine X-ray crystallography with all-atom molecular dynamics simulations to elucidate the structure of the precatalytic complex of human DHHC20 in complex with palmitoyl CoA. The resulting structure reveals that the fatty acyl chain inserts into a hydrophobic pocket within the transmembrane spanning region of the protein, whereas the CoA headgroup is recognized by the cytosolic domain through polar and ionic interactions. Biochemical experiments corroborate the predictions from our structural model. We show, using both computational and experimental analyses, that palmitoyl CoA acts as a bivalent ligand where the interaction of the DHHC enzyme with both the fatty acyl chain and the CoA headgroup is important for catalytic chemistry to proceed. This bivalency explains how, in the presence of high concentrations of free CoA under physiological conditions, DHHC enzymes can efficiently use palmitoyl CoA as a substrate for autoacylation.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.