Evidence map›Paper›PMID 27760376›Full record

ArticleCellular signalling2017

Discovery of new substrates of the elongation factor-2 kinase suggests a broader role in the cellular nutrient response.

Michael B Lazarus, Rebecca S Levin, Kevan M Shokat

Open access · greenAbstract read
In one paragraph

Article in Cellular signalling, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.9field-weighted citation impact, top 23% 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

12 citing papers in PubMed, 22 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

3 authors at 2 institutions in 1 country.

Michael B LazarusHoward Hughes Medical Institute and Department of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, CA 94158, USA.
Rebecca S LevinHoward Hughes Medical Institute and Department of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, CA 94158, USA.
Kevan M ShokatHoward Hughes Medical Institute and Department of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, CA 94158, USA. Electronic address: kevan.shokat@ucsf.edu.
Howard Hughes Medical Institute · USUniversity of California, San Francisco · US

Funding

Translational Incubator CoreU19AI109662 · NIAID · STANFORD UNIVERSITY · PI GLENN, JEFFREY S · 2014 to 2019
$28.6M
Bio-Organic Biomedical Mass Spectromy ResourceP41GM103481 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BURLINGAME, ALMA L · 2012 to 2015
$6.4M
The PIP2-virus interface and PI 4-kinase: novel biology and validation targetsR01AI099245 · NIAID · STANFORD UNIVERSITY · PI GLENN, JEFFREY S · 2012 to 2016
$5.2M
Targeting nutrient-sensing pathways in cancerK22CA201103 · NCI · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI LAZARUS, MICHAEL BLOCK · 2016 to 2017
$382k
Howard Hughes Medical InstituteNCI NIH HHS K22 CA201103NIAID NIH HHS R01 AI099245NIAID NIH HHS U19 AI109662NIGMS NIH HHS P41 GM103481
6 · The paper itself

Abstract

Elongation Factor-2 Kinase (eEF2K) in an unusual mammalian enzyme that has one known substrate, elongation factor-2. It belongs to a class of kinases, called alpha kinases, that has little sequence identity to the >500 conventional protein kinases, but performs the same reaction and has similar catalytic residues. The phosphorylation of eEF2 blocks translation elongation, which is thought to be critical to regulating cellular energy usage. Here we report a system for discovering new substrates of alpha kinases and identify the first new substrates of eEF2K including AMPK and alpha4, and determine a sequence motif for the kinase that shows a requirement for threonine residues as the target of phosphorylation. These new substrates suggest that eEF2K has a more diverse role in regulating cellular energy usage that involves multiple pathways and regulatory feedback.

Indexed as

Amino Acid SequenceCellsComputational BiologyElongation Factor 2 KinaseHeLa CellsHumansPeptidesPhosphorylationReproducibility of ResultsSubstrate SpecificityEEF2K protein, humanElongation Factor 2 KinasePeptidesalpha4AMPKeEF2eEF2KEnergy homeostasisTranslation elongation

Identifiers

PMID27760376
PMCPMC5138099
OpenAlexW2532198414

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.