Stearic acid blunts growth-factor signaling via oleoylation of GNAI proteins
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 tha...
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| Hauptverfasser: | , , , , , , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
28 July 2021
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| In: |
Nature Communications
Year: 2021, Jahrgang: 12, Pages: 1-15 |
| ISSN: | 2041-1723 |
| DOI: | 10.1038/s41467-021-24844-9 |
| Online-Zugang: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1038/s41467-021-24844-9 Verlag, lizenzpflichtig, Volltext: http://www.nature.com/articles/s41467-021-24844-9 
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| Verfasserangaben: | Hana Nůsková, Marina V. Serebryakova, Anna Ferrer-Caelles, Timo Sachsenheimer, Christian Lüchtenborg, Aubry K. Miller, Britta Brügger, Larisa V. Kordyukova & Aurelio A. Teleman |
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| 245 | 1 | 0 | |a Stearic acid blunts growth-factor signaling via oleoylation of GNAI proteins |c Hana Nůsková, Marina V. Serebryakova, Anna Ferrer-Caelles, Timo Sachsenheimer, Christian Lüchtenborg, Aubry K. Miller, Britta Brügger, Larisa V. Kordyukova & Aurelio A. Teleman |
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| 520 | |a 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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