Evidence map›Paper›PMID 31120171›Full record

ArticleThe FEBS journal2019

Phosphorylation of Arabidopsis eIF4E and eIFiso4E by SnRK1 inhibits translation.

Aaron N Bruns, Sizhun Li, Gireesha Mohannath, David M Bisaro

Open access · bronzeAbstract read
In one paragraph

Article in The FEBS journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
6.4field-weighted citation impact, top 4% 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

20 citing papers in PubMed, 36 citations in OpenAlex.

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  12. Dynamic Nutrient Signaling Networks in Plants.Annual review of cell and developmental biology · 2021
    Review
  13. Article
  14. Translational gene regulation in plants: A green new deal.Wiley interdisciplinary reviews. RNA · 2020
    Review
  15. Characterization of Local and Systemic Impact of Whitefly (International journal of molecular sciences · 2020
    Article
  16. Article
  17. Evidence That Phosphorylation of theFrontiers in plant science · 2020
    Article
  18. Review
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Aaron N BrunsDepartment of Molecular Genetics, Center for Applied Plant Sciences, Center for RNA Biology, and Infectious Diseases Institute, The Ohio State University, Columbus, OH, USA.
Sizhun LiDepartment of Molecular Genetics, Center for Applied Plant Sciences, Center for RNA Biology, and Infectious Diseases Institute, The Ohio State University, Columbus, OH, USA.
Gireesha MohannathDepartment of Molecular Genetics, Center for Applied Plant Sciences, Center for RNA Biology, and Infectious Diseases Institute, The Ohio State University, Columbus, OH, USA.
David M BisaroDepartment of Molecular Genetics, Center for Applied Plant Sciences, Center for RNA Biology, and Infectious Diseases Institute, The Ohio State University, Columbus, OH, USA.
Institute for Behavioral Medicine · USThe Ohio State University · US

Funding

Cellular, molecular, and biochemical sciences training grantT32GM086252 · NIGMS · OHIO STATE UNIVERSITY · PI JACKMAN, JANE ELIZABETH, MUSIER-FORSYTH, KARIN M · 2011 to 2020
$2.0M
A Systems Biology Approach for Targeted Drug Discovery for LeishmaniasisR21AI127582 · NIAID · OHIO STATE UNIVERSITY · PI IBBA, MICHAEL, SATOSKAR, ABHAY R · 2017 to 2018
$401k
Division of Integrative Organismal Systems, National Science Foundation IOS-1354636Division of Molecular and Cellular Biosciences, National Science Foundation MCB-1158262National Institute of Food and Agriculture 2015--6703-22999NIAID NIH HHS R21 AI127582NIGMS NIH HHS T32 GM086252OSU Center for Applied Plant Sciences (CAPS)
6 · The paper itself

Abstract

Regulation of protein synthesis is critical for maintaining cellular homeostasis. In mammalian systems, translational regulatory networks have been elucidated in considerable detail. In plants, however, regulation occurs through different mechanisms that remain largely elusive. In this study, we present evidence that the Arabidopsis thaliana energy sensing kinase SnRK1, a homologue of mammalian AMP-activated kinase and yeast sucrose non-fermenting 1 (SNF1), inhibits translation by phosphorylating the cap binding proteins eIF4E and eIFiso4E. We establish that eIF4E and eIFiso4E contain two deeply conserved SnRK1 consensus target sites and that both interact with SnRK1 in vivo. We then demonstrate that SnRK1 phosphorylation inhibits the ability of Arabidopsis eIF4E and eIFiso4E to complement a yeast strain lacking endogenous eIF4E, and that inhibition correlates with repression of polysome formation. Finally, we show that SnRK1 over-expression in Nicotiana benthamiana plants reduces polysome formation, and that this effect can be counteracted by transient expression of eIF4E or mutant eIF4E containing non-phosphorylatable SnRK1 target residues, but not by a phosphomimic eIF4E. Together, these studies elucidate a novel and direct pathway for translational control in plant cells. In light of previous findings that SnRK1 conditions an innate antiviral defense and is inhibited by geminivirus pathogenicity factors, we speculate that phosphorylation of cap binding proteins may be a component of the resistance mechanism.

Indexed as

Protein BiosynthesisArabidopsisArabidopsis ProteinsEukaryotic Initiation Factor-4EPhosphorylationPolyribosomesProtein Serine-Threonine KinasesArabidopsis ProteinsAt3g01090 protein, ArabidopsisEukaryotic Initiation Factor-4EProtein Serine-Threonine KinaseseIF4EeIFiso4EgeminivirusSnRK1translation

Identifiers

PMID31120171
PMCPMC6779489
OpenAlexW2946007256

What OpenQuestion holds

Textmetadata
LicenceTDM
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.