Evidence map›Paper›PMID 35140179›Full record

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.

Chul-Jin Lee, Robyn Stix, Mitra S Rana, Flowreen Shikwana, R Elliot Murphy, Rodolfo Ghirlando, José D Faraldo-Gómez, Anirban Banerjee

Open access · hybridAbstract read
In one paragraph

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.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.5field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

21 citing papers in PubMed, 30 citations in OpenAlex.

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  11. Mechanisms and functions of protein S-acylation.Nature reviews. Molecular cell biology · 2024
    Review
  12. Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. Review
  18. The Mechanism of Selective Recognition of Lipid Substrate by hDHHC20 Enzyme.International journal of molecular sciences · 2022
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 4 institutions in 1 country.

Chul-Jin LeeSection on Structural and Chemical Biology of Membrane Proteins, Eunice Kennedy Shriver National Institute of Child Health and Human Development, NIH, Bethesda, MD 20892.
Robyn StixTheoretical Molecular Biophysics Laboratory, National Heart, Lung and Blood Institute, NIH, Bethesda, MD 20892.ORCID 0000-0003-2128-7875
Mitra S RanaSection on Structural and Chemical Biology of Membrane Proteins, Eunice Kennedy Shriver National Institute of Child Health and Human Development, NIH, Bethesda, MD 20892.ORCID 0000-0002-0915-8141
Flowreen ShikwanaSection on Structural and Chemical Biology of Membrane Proteins, Eunice Kennedy Shriver National Institute of Child Health and Human Development, NIH, Bethesda, MD 20892.
R Elliot MurphySection on Structural and Chemical Biology of Membrane Proteins, Eunice Kennedy Shriver National Institute of Child Health and Human Development, NIH, Bethesda, MD 20892.ORCID 0000-0002-4144-2345
Rodolfo GhirlandoLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, NIH, Bethesda, MD 20892.ORCID 0000-0003-4880-4959
José D Faraldo-GómezTheoretical Molecular Biophysics Laboratory, National Heart, Lung and Blood Institute, NIH, Bethesda, MD 20892; jose.faraldo@nih.gov anirban.banerjee@nih.gov.ORCID 0000-0001-7224-7676
Anirban BanerjeeSection on Structural and Chemical Biology of Membrane Proteins, Eunice Kennedy Shriver National Institute of Child Health and Human Development, NIH, Bethesda, MD 20892; jose.faraldo@nih.gov anirban.banerjee@nih.gov.ORCID 0000-0003-1494-6801
Eunice Kennedy Shriver National Institute of Child Health and Human Development · USJohns Hopkins University · USNational Heart Lung and Blood Institute · USNational Institute of Diabetes and Digestive and Kidney Diseases · US

Funding

Structural and chemical biology of membrane proteinsZIAHD008928 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI BANERJEE, ANIRBAN · 2013 to 2025
$34.5M
User Training & OutreachP30GM138396 · NIGMS · UCHICAGO ARGONNE, LLC · PI ROBERT F. FISCHETTI, JANET L. SMITH · 2020 to 2026
$34.3M
User Training and OutreachP30GM124165 · NIGMS · CORNELL UNIVERSITY · PI Nozomi Ando, J Christopher Fromme · 2018 to 2026
$34.2M
structural characterization of bacterial secretion channelsZIADK036139 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BUCHANAN, SUSAN · 2009 to 2025
$19.3M
Molecular Mechanisms in Membrane Bioenergetics, Transport and SignalingZIAHL006203 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI FARALDO-GÓMEZ, JOSE · 2015 to 2023
$15.4M
Biophysics of Macromolecular ComplexesZIADK033007 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BUCHANAN, SUSAN · 2009 to 2024
$4.9M
Pixel Array Detector for Macromolecular CrystallographyS10OD021527 · OD · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2016 to 2016
$2.0M
High-Speed High-Sensitivity Detector for X-ray Micro-Crystallography at GM/CA@APSS10OD012289 · OD · UNIVERSITY OF CHICAGO · PI FISCHETTI, ROBERT F. · 2014 to 2014
$2.0M
Intramural NIH HHS ZIA DK036139Intramural NIH HHS ZIA HD008928NIGMS NIH HHS P30 GM124165NIGMS NIH HHS P30 GM138396NIH HHS S10 OD012289NIH HHS S10 OD021527
6 · The paper itself

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.

Indexed as

Acyl Coenzyme AAcyltransferasesCatalytic DomainCell MembraneGene Expression Regulation, EnzymologicHumansLipoylationModels, MolecularMolecular Dynamics SimulationMutationProtein BindingProtein ConformationProtein DomainsAcyl Coenzyme AAcyltransferasesZDHHC20 protein, humanDHHC acyltransferasefatty acyl-CoAintegral membrane enzymemembrane protein structureprotein S-acylation

Identifiers

PMID35140179
PMCPMC8851515
OpenAlexW4211102344

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

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.