Evidence map›Paper›PMID 24240988›Full record

ArticleNature communications2013

Autophagy proteins regulate ERK phosphorylation.

Nuria Martinez-Lopez, Diana Athonvarangkul, Priti Mishall, Srabani Sahu, Rajat Singh

Open access · hybridAbstract read
In one paragraph

Article in Nature communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 152 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
152citing papers in PubMed, 1 pooled it
13.4field-weighted citation impact, top 1% 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

152 citing papers in PubMed, 1 synthesis or guideline pooled it, 247 citations in OpenAlex.

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92 more citing papers are in PubMed but not listed here.

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

5 authors at 1 institution in 1 country.

Nuria Martinez-Lopez1] Department of Medicine, Albert Einstein College of Medicine, Bronx, New York 10461, USA [2] Department of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
Diana Athonvarangkul
Priti Mishall
Srabani Sahu
Rajat Singh
Albert Einstein College of Medicine · US

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM007288 · NIGMS · YESHIVA UNIVERSITY · PI AKABAS, MYLES H. · 1985 to 2022
$35.6M
Stable Isotope and Metabolomics CoreP60DK020541 · NIDDK · YESHIVA UNIVERSITY · PI PESSIN, JEFFREY E. · 1986 to 2014
$29.8M
Translational Research CoreP30DK020541 · NIDDK · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI JILL CRANDALL · 2015 to 2026
$27.7M
Hypothalamic Autophagy and Metabolic Regulation in AgingR01AG043517 · NIA · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI Rajat Singh · 2013 to 2026
$2.3M
Hyptothalamic autophagy and metabolic regulation in agingRF1AG043517 · NIA · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI SINGH, RAJAT · 2019 to 2019
$2.1M
Regulation of lipid metabolism by macroautophagyK01DK087776 · NIDDK · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI SINGH, RAJAT · 2010 to 2014
$605k
NIA NIH HHS AG043517NIA NIH HHS R01 AG043517NIA NIH HHS RF1 AG043517NIDDK NIH HHS DK020541NIDDK NIH HHS DK087776NIDDK NIH HHS K01 DK087776NIDDK NIH HHS P30 DK020541NIDDK NIH HHS P60 DK020541NIGMS NIH HHS 5T32GM728837NIGMS NIH HHS T32 GM007288
6 · The paper itself

Abstract

Autophagy is a conserved pathway that maintains cellular quality control. Extracellular signal-regulated kinase (ERK) controls various aspects of cell physiology including proliferation. Multiple signalling cascades, including ERK, have been shown to regulate autophagy, however whether autophagy proteins (ATG) regulate cell signalling is unknown. Here we show that growth factor exposure increases the interaction of ERK cascade components with ATG proteins in the cytosol and nucleus. ERK and its upstream kinase MEK localize to the extra-luminal face of autophagosomes. ERK2 interacts with ATG proteins via its substrate-binding domains. Deleting Atg7 or Atg5 or blocking LC3 lipidation or ATG5-ATG12 conjugation decreases ERK phosphorylation. Conversely, increasing LC3-II availability by silencing the cysteine protease ATG4B or acute trehalose exposure increases ERK phosphorylation. Decreased ERK phosphorylation in Atg5⁻/⁻ cells does not occur from overactive phosphatases. Our findings thus reveal an unconventional function of ATG proteins as cellular scaffolds in the regulation of ERK phosphorylation.

Indexed as

AnimalsAutophagyAutophagy-Related Protein 5Autophagy-Related Protein 7Autophagy-Related ProteinsCell LineCysteine EndopeptidasesDown-RegulationExtracellular Signal-Regulated MAP KinasesMaleMiceMicrotubule-Associated ProteinsMitogen-Activated Protein Kinase KinasesPhosphorylationAtg4b protein, mouseAtg5 protein, mouseAtg7 protein, mouseAutophagy-Related Protein 5Autophagy-Related Protein 7Autophagy-Related ProteinsCysteine EndopeptidasesExtracellular Signal-Regulated MAP KinasesMap1lc3b protein, mouseMicrotubule-Associated ProteinsMitogen-Activated Protein Kinase Kinases

Identifiers

PMID24240988
PMCPMC3868163
OpenAlexW1979952830

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.