ArticleNature communications2021
Stearic acid blunts growth-factor signaling via oleoylation of GNAI proteins.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 38 citations in OpenAlex.
- Lipid Metabolic Labeling to Study Site- and Lipid-Specific Long-ChainACS chemical biology · 2026Article
- Gαi1 and Gαi3 mediate IL-11-induced signal transduction and are potential therapeutic targets for LUAD.Cell death & disease · 2026Article
- Enzyme-centric chemoproteomics reveals isomer-specific S-acylation modification networks.Nature communications · 2026Article
- Integrative Analysis of Multiomic Pathways Predicts Cancer-Affected Lobes in Lung Cancer.Cancer prevention research (Philadelphia, Pa.) · 2026Article
- Metabolites beyond metabolism: Exploring their atypical roles in protein modification and signaling transduction.Chinese medical journal · 2026Review
- Targeting GNG4 inhibits tumor progression and restores enzalutamide sensitivity in prostate cancer by suppressing autophagy.Cell death & disease · 2026Article
- Targeting metabolic-epigenetic-immune axis in cancer: molecular mechanisms and therapeutic implications.Signal transduction and targeted therapy · 2026Review
- Exploring Lipid Metabolic Reprogramming: Mechanistic Insights and Implications for Tumor Radiotherapy.International journal of biological sciences · 2026Review
- Oleate activates PLD2 lipase and GEF activity by modulating membrane microdomain dynamics via S-acylation.Journal of lipid research · 2025Article
- Pharmacological induction of acetyl-CoA carboxylase 1 autophagic degradation attenuates lipid accumulation and cholangiocarcinoma progression.Journal of experimental & clinical cancer research : CR · 2025Article
- Anti-Inflammatory Activity and Mechanism of Stearic Acid Extract From Purslane.Food science & nutrition · 2025Article
- Mechanisms of metabolism-coupled protein modifications.Nature chemical biology · 2025Review
- Capillary Zone Electrophoresis-Mass Spectrometry of Intact G Protein-Coupled Receptors Enables Proteoform Profiling.Analytical chemistry · 2025Article
- Specificity of mRNA binding to proteins within the NMD machinery is influenced in cancer.Frontiers in molecular biosciences · 2025Article
- Quantitative analysis of protein lipidation and acyl-CoAs reveals substrate preferences of theChemical science · 2024Article
- Enrichment of C17:0-rich saturated fatty acids from sheep tail fat for adjuvant therapy of non-small-cell lung cancer.Food science and biotechnology · 2024Article
- Comparative Analysis of the GNAI Family Genes in Glioblastoma through Transcriptomics and Single-Cell Technologies.Cancers · 2023Article
- Beyond the G protein α subunit: investigating the functional impact of other components of the GαiCell communication and signaling : CCS · 2023Article
- Lactate-induced protein lactylation: A bridge between epigenetics and metabolic reprogramming in cancer.Cell proliferation · 2023Review
- The Mechanism of Selective Recognition of Lipid Substrate by hDHHC20 Enzyme.International journal of molecular sciences · 2022Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Covalent attachment of C16:0 to proteins (palmitoylation) regulates protein function. Proteins are also S-acylated by other fatty acids including C18:0. Whether protein acylation with different fatty acids has different functional outcomes is not well studied. We show here that C18:0 (stearate) and C18:1 (oleate) compete with C16:0 to S-acylate Cys3 of GNAI proteins. C18:0 becomes desaturated so that C18:0 and C18:1 both cause S-oleoylation of GNAI. Exposure of cells to C16:0 or C18:0 shifts GNAI acylation towards palmitoylation or oleoylation, respectively. Oleoylation causes GNAI proteins to shift out of cell membrane detergent-resistant fractions where they potentiate EGFR signaling. Consequently, exposure of cells to C18:0 reduces recruitment of Gab1 to EGFR and reduces AKT activation. This provides a molecular mechanism for the anti-tumor effects of C18:0, uncovers a mechanistic link how metabolites affect cell signaling, and provides evidence that the identity of the fatty acid acylating a protein can have functional consequences.
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Registered trials
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.