Evidence map›Paper›PMID 35841486›Full record

ArticleCellular and molecular life sciences : CMLS2022

Ghrelin rapidly elevates protein synthesis in vitro by employing the rpS6K-eEF2K-eEF2 signalling axis.

Alexander V Zhdanov, Anna V Golubeva, Martina M Yordanova, Dmitry E Andreev, Ana Paula Ventura-Silva, Harriet Schellekens, Pavel V Baranov, John F Cryan, Dmitri B Papkovsky

Open access · hybridAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 55% 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

2 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. Review
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.

Alexander V ZhdanovSchool of Biochemistry & Cell Biology, University College Cork, Cavanagh Pharmacy Building, College Road, Cork, Ireland. a.zhdanov@ucc.ie.ORCID http://orcid.org/0000-0001-5787-2035
Anna V GolubevaDepartment of Anatomy & Neuroscience, University College Cork, Cork, Ireland.
Martina M YordanovaSchool of Biochemistry & Cell Biology, University College Cork, Cavanagh Pharmacy Building, College Road, Cork, Ireland.
Dmitry E AndreevBelozersky Research Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, Russia.
Ana Paula Ventura-SilvaAPC Microbiome Institute, University College Cork, Cork, Ireland.
Harriet SchellekensDepartment of Anatomy & Neuroscience, University College Cork, Cork, Ireland.
Pavel V BaranovSchool of Biochemistry & Cell Biology, University College Cork, Cavanagh Pharmacy Building, College Road, Cork, Ireland.
John F CryanDepartment of Anatomy & Neuroscience, University College Cork, Cork, Ireland.
Dmitri B PapkovskySchool of Biochemistry & Cell Biology, University College Cork, Cavanagh Pharmacy Building, College Road, Cork, Ireland.
University College Cork · IELomonosov Moscow State University · RUUniversity College Dublin · IE

Funding

Science Foundation Ireland 12/RC/2273Science Foundation Ireland 12/RC/2276SFI-HRB-Wellcome Trust Biomedical Research Partnership 210692/Z/18/ZWellcome Trust
6 · The paper itself

Abstract

Activated ghrelin receptor GHS-R1α triggers cell signalling pathways that modulate energy homeostasis and biosynthetic processes. However, the effects of ghrelin on mRNA translation are unknown. Using various reporter assays, here we demonstrate a rapid elevation of protein synthesis in cells within 15-30 min upon stimulation of GHS-R1α by ghrelin. We further show that ghrelin-induced activation of translation is mediated, at least in part, through the de-phosphorylation (de-suppression) of elongation factor 2 (eEF2). The levels of eEF2 phosphorylation at Thr56 decrease due to the reduced activity of eEF2 kinase, which is inhibited via Ser366 phosphorylation by rpS6 kinases. Being stress-susceptible, the ghrelin-mediated decrease in eEF2 phosphorylation can be abolished by glucose deprivation and mitochondrial uncoupling. We believe that the observed burst of translation benefits rapid restocking of neuropeptides, which are released upon GHS-R1α activation, and represents the most time- and energy-efficient way of prompt recharging the orexigenic neuronal circuitry.

Indexed as

GhrelinProtein BiosynthesisPeptide Elongation Factor 2PhosphorylationSignal TransductionGhrelinPeptide Elongation Factor 2Cell signallingDe novo protein productioneEF2 phosphorylationGhrelin receptor GHS-R1αTranslation elongation

Identifiers

PMID35841486
PMCPMC9288388
OpenAlexW4285588535

What OpenQuestion holds

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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.