Evidence map›Paper›PMID 29795412›Full record

ArticleScientific reports2018

Effects of single amino acid deficiency on mRNA translation are markedly different for methionine versus leucine.

Kevin M Mazor, Leiming Dong, Yuanhui Mao, Robert V Swanda, Shu-Bing Qian, Martha H Stipanuk

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

39 citing papers in PubMed, 63 citations in OpenAlex.

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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

6 authors at 1 institution in 1 country.

Kevin M MazorDivision of Nutritional Sciences, Cornell University, Ithaca, NY, 14853, USA.
Leiming DongDivision of Nutritional Sciences, Cornell University, Ithaca, NY, 14853, USA.
Yuanhui MaoDivision of Nutritional Sciences, Cornell University, Ithaca, NY, 14853, USA.
Robert V SwandaDivision of Nutritional Sciences, Cornell University, Ithaca, NY, 14853, USA.
Shu-Bing QianDivision of Nutritional Sciences, Cornell University, Ithaca, NY, 14853, USA.ORCID 0000-0002-4127-1136
Martha H StipanukDivision of Nutritional Sciences, Cornell University, Ithaca, NY, 14853, USA. mhs6@cornell.edu.
Cornell University · US

Funding

Translational Research CoreP30DK020541 · NIDDK · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI STREAMSON C CHUA · 2015 to 2026
$27.7M
Linking Nutrient Signaling and Protein Homeostasis in Mammalian AgingR01AG042400 · NIA · CORNELL UNIVERSITY · PI QIAN, SHU-BING · 2013 to 2017
$1.6M
O-GlcNAc Signaling in Translational Control of Stress ResponseR01GM122814 · NIGMS · CORNELL UNIVERSITY · PI QIAN, SHU-BING · 2017 to 2020
$1.3M
Cross-talk between GCN2 and mTOR in integration of nutrient signalingR56DK083473 · NIDDK · CORNELL UNIVERSITY · PI STIPANUK, MARTHA H · 2009 to 2009
$193k
NIA NIH HHS R01 AG042400NIDDK NIH HHS P30 DK020541NIDDK NIH HHS R56 DK083473NIGMS NIH HHS R01 GM122814
6 · The paper itself

Abstract

Although amino acids are known regulators of translation, the unique contributions of specific amino acids are not well understood. We compared effects of culturing HEK293T cells in medium lacking either leucine, methionine, histidine, or arginine on eIF2 and 4EBP1 phosphorylation and measures of mRNA translation. Methionine starvation caused the most drastic decrease in translation as assessed by polysome formation, ribosome profiling, and a measure of protein synthesis (puromycin-labeled polypeptides) but had no significant effect on eIF2 phosphorylation, 4EBP1 hyperphosphorylation or 4EBP1 binding to eIF4E. Leucine starvation suppressed polysome formation and was the only tested condition that caused a significant decrease in 4EBP1 phosphorylation or increase in 4EBP1 binding to eIF4E, but effects of leucine starvation were not replicated by overexpressing nonphosphorylatable 4EBP1. This suggests the binding of 4EBP1 to eIF4E may not by itself explain the suppression of mRNA translation under conditions of leucine starvation. Ribosome profiling suggested that leucine deprivation may primarily inhibit ribosome loading, whereas methionine deprivation may primarily impair start site recognition. These data underscore our lack of a full understanding of how mRNA translation is regulated and point to a unique regulatory role of methionine status on translation initiation that is not dependent upon eIF2 phosphorylation.

Indexed as

Adaptor Proteins, Signal TransducingAmino AcidsCell Cycle ProteinsCulture MediaEukaryotic Initiation Factor-2Eukaryotic Initiation Factor-4EHEK293 CellsHumansLeucineMethioninePhosphoproteinsPhosphorylationProtein BiosynthesisRibosomesRNA, MessengerAdaptor Proteins, Signal TransducingAmino AcidsCell Cycle ProteinsCulture MediaEIF4EBP1 protein, humanEukaryotic Initiation Factor-2Eukaryotic Initiation Factor-4ELeucineMethioninePhosphoproteinsRNA, Messenger

Identifiers

PMID29795412
PMCPMC5967319
OpenAlexW2806887154

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.