Evidence map›Paper›PMID 34321466›Full record

ArticleNature communications2021

Stearic acid blunts growth-factor signaling via oleoylation of GNAI proteins.

Hana Nůsková, Marina V Serebryakova, Anna Ferrer-Caelles, Timo Sachsenheimer, Christian Lüchtenborg, Aubry K Miller, Britta Brügger, Larisa V Kordyukova, Aurelio A Teleman

Open access · goldAbstract read
In one paragraph

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.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.8field-weighted citation impact, top 8% 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

23 citing papers in PubMed, 38 citations in OpenAlex.

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  20. The Mechanism of Selective Recognition of Lipid Substrate by hDHHC20 Enzyme.International journal of molecular sciences · 2022
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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

9 authors at 3 institutions in 2 countries.

Hana NůskováGerman Cancer Research Center (DKFZ), Heidelberg, Germany.ORCID 0000-0002-5562-9207
Marina V Serebryakova *A.N. Belozersky Institute of Physico-Chemical Biology, M.V. Lomonosov Moscow State University, Moscow, Russia.ORCID 0000-0002-5402-8215
Anna Ferrer-Caelles *German Cancer Research Center (DKFZ), Heidelberg, Germany.ORCID 0000-0002-2037-4101
Timo SachsenheimerHeidelberg University Biochemistry Center (BZH), Heidelberg, Germany.
Christian LüchtenborgHeidelberg University Biochemistry Center (BZH), Heidelberg, Germany.
Aubry K MillerGerman Cancer Research Center (DKFZ), Heidelberg, Germany.ORCID 0000-0002-1761-4143
Britta BrüggerHeidelberg University Biochemistry Center (BZH), Heidelberg, Germany.ORCID 0000-0002-3477-8270
Larisa V KordyukovaA.N. Belozersky Institute of Physico-Chemical Biology, M.V. Lomonosov Moscow State University, Moscow, Russia.ORCID 0000-0002-6089-1103
Aurelio A TelemanGerman Cancer Research Center (DKFZ), Heidelberg, Germany. a.teleman@dkfz.de.ORCID 0000-0002-4237-9368
German Cancer Research Center · DEHeidelberg University · DELomonosov Moscow State University · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

AcylationCell MembraneCell ProliferationFatty AcidsGTP-Binding Protein alpha Subunits, Gi-GoHumansIntercellular Signaling Peptides and ProteinsLipoylationMCF-7 CellsOleic AcidsSignal TransductionStearic AcidsFatty AcidsGNAI1 protein, humanGNAI3 protein, humanGTP-Binding Protein alpha Subunits, Gi-GoIntercellular Signaling Peptides and ProteinsOleic Acidsstearic acidStearic Acids

Identifiers

PMID34321466
PMCPMC8319428
OpenAlexW3186997119

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.