Evidence map›Paper›PMID 26169956›Full record

ArticleCellular signalling2015

The mechanism and function of mitogen-activated protein kinase activation by ARF1.

Fuguo Zhou, Chunmin Dong, Jason E Davis, William H Wu, Kristen Surrao, Guangyu Wu

Open access · greenAbstract read
In one paragraph

Article in Cellular signalling, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

14 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Journal of medical genetics · 2023
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  10. Recombinant protein ofOncotarget · 2017
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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 2 institutions in 1 country.

Fuguo Zhou *Department of Pharmacology and Experimental Therapeutics, Louisiana State University Health Sciences Center, 1901 Perdido St, New Orleans, LA 70112, United States.
Chunmin Dong *Department of Pharmacology and Experimental Therapeutics, Louisiana State University Health Sciences Center, 1901 Perdido St, New Orleans, LA 70112, United States.
Jason E DavisDepartment of Pharmacology and Toxicology, Medical College of Georgia, Georgia Regents University, 1459 Laney Walker Blvd., Augusta, GA 30912, United States.
William H WuDepartment of Pharmacology and Toxicology, Medical College of Georgia, Georgia Regents University, 1459 Laney Walker Blvd., Augusta, GA 30912, United States.
Kristen SurraoDepartment of Pharmacology and Toxicology, Medical College of Georgia, Georgia Regents University, 1459 Laney Walker Blvd., Augusta, GA 30912, United States.
Guangyu WuDepartment of Pharmacology and Experimental Therapeutics, Louisiana State University Health Sciences Center, 1901 Perdido St, New Orleans, LA 70112, United States.
Augusta University · USLouisiana State University Health Sciences Center New Orleans · US

Funding

ER-to-Golgi traffic and signal regulation of GPCRsR01GM076167 · NIGMS · LSU HEALTH SCIENCES CENTER · PI WU, GUANGYU · 2006 to 2013
$2.2M
NIGMS NIH HHS R01 GM076167NIGMS NIH HHS R01GM076167
6 · The paper itself

Abstract

Mitogen-activated protein kinases (MAPK) can be activated by a number of biochemical pathways through distinct signaling molecules. We have recently revealed a novel function for the Ras-like small GTPase ADP-ribosylation factor 1 (ARF1) in mediating the activation of Raf1-MEK-ERK1/2 pathway by G protein-coupled receptors [Dong C, Li C and Wu G (2011) J Biol Chem 286, 43,361-43,369]. Here, we have further defined the underlying mechanism and the possible function of ARF1-mediated MAPK pathway. We demonstrated that the blockage of ARF1 activation and the disruption of ARF1 localization to the Golgi by mutating Thr48, a highly conserved residue involved in the exchange of GDP for GTP, and the myristoylation site Gly2 abolished ARF1's ability to activate ERK1/2. In addition, treatment with Golgi structure disrupting agents markedly attenuated ARF1-mediated ERK1/2 activation. Furthermore, ARF1 significantly promoted cell proliferation. More interestingly, ARF1 activated 90kDa ribosomal S6 kinase 1 (RSK1) without influencing Elk-1 activation and ERK2 translocation to the nuclei. These data demonstrate that, once activated, ARF1 activates the MAPK pathway likely using the Golgi as a main platform, which in turn activates the cytoplasmic RSK1, leading to cell proliferation.

Indexed as

ADP-Ribosylation Factor 1Amino Acid SequenceCell ProliferationEnzyme Activationets-Domain Protein Elk-1Extracellular Signal-Regulated MAP KinasesGolgi ApparatusHEK293 CellsHumansMAP Kinase Signaling SystemProtein TransportReceptor, Adenosine A2BRibosomal Protein S6 Kinases, 90-kDaADP-Ribosylation Factor 1ELK1 protein, humanets-Domain Protein Elk-1Extracellular Signal-Regulated MAP KinasesReceptor, Adenosine A2BRibosomal Protein S6 Kinases, 90-kDaRPS6KA1 protein, humanARF1Cell proliferationERK1/2G proteinG protein-coupled receptorMAPKRSK1

Identifiers

PMID26169956
PMCPMC4739547
OpenAlexW2282774637

What OpenQuestion holds

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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.