Evidence map›Paper›PMID 16805921›Full record

ArticleJournal of biology2006

ERK1 and ERK2 mitogen-activated protein kinases affect Ras-dependent cell signaling differentially.

Chiara Vantaggiato, Ivan Formentini, Attilio Bondanza, Chiara Bonini, Luigi Naldini, Riccardo Brambilla

Open access · goldAbstract read
In one paragraph

Article in Journal of biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 110 papers.

0numbers the graph read from it
0cells of the map it votes in
110citing papers in PubMed
8.1field-weighted citation impact, top 2% 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

110 citing papers in PubMed, 208 citations in OpenAlex.

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  8. Review
  9. Growth Inhibitory Signaling of the Raf/MEK/ERK Pathway.International journal of molecular sciences · 2020
    Review
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  15. Article
  16. Efficient farnesylation of an extended C-terminal C(The Journal of biological chemistry · 2018
    Article
  17. Article
  18. Article
  19. Article
  20. Article

50 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

6 authors at 1 institution in 1 country.

Chiara Vantaggiato *Istituto Scientifico San Raffaele and Università Vita-Salute San Raffaele, Via Olgettina 58, 20132 Milano, Italy.
Ivan Formentini *Istituto Scientifico San Raffaele and Università Vita-Salute San Raffaele, Via Olgettina 58, 20132 Milano, Italy.
Attilio BondanzaIstituto Scientifico San Raffaele and Università Vita-Salute San Raffaele, Via Olgettina 58, 20132 Milano, Italy.
Chiara BoniniIstituto Scientifico San Raffaele and Università Vita-Salute San Raffaele, Via Olgettina 58, 20132 Milano, Italy.
Luigi NaldiniIstituto Scientifico San Raffaele and Università Vita-Salute San Raffaele, Via Olgettina 58, 20132 Milano, Italy.
Riccardo BrambillaIstituto Scientifico San Raffaele and Università Vita-Salute San Raffaele, Via Olgettina 58, 20132 Milano, Italy.
Vita-Salute San Raffaele University · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe mitogen-activated protein (MAP) kinases p44ERK1 and p42ERK2 are crucial components of the regulatory machinery underlying normal and malignant cell proliferation. A currently accepted model maintains that ERK1 and ERK2 are regulated similarly and contribute to intracellular signaling by phosphorylating a largely common subset of substrates, both in the cytosol and in the nucleus.

resultsHere, we show that ablation of ERK1 in mouse embryo fibroblasts and NIH 3T3 cells by gene targeting and RNA interference results in an enhancement of ERK2-dependent signaling and in a significant growth advantage. By contrast, knockdown of ERK2 almost completely abolishes normal and Ras-dependent cell proliferation. Ectopic expression of ERK1 but not of ERK2 in NIH 3T3 cells inhibits oncogenic Ras-mediated proliferation and colony formation. These phenotypes are independent of the kinase activity of ERK1, as expression of a catalytically inactive form of ERK1 is equally effective. Finally, ectopic expression of ERK1 but not ERK2 is sufficient to attenuate Ras-dependent tumor formation in nude mice.

conclusionThese results reveal an unexpected interplay between ERK1 and ERK2 in transducing Ras-dependent cell signaling and proliferation. Whereas ERK2 seems to have a positive role in controlling normal and Ras-dependent cell proliferation, ERK1 probably affects the overall signaling output of the cell by antagonizing ERK2 activity.

Indexed as

Signal TransductionAnimalsCell ProliferationCells, CulturedEnzyme ActivationGene SilencingMiceMice, NudeMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Mitogen-Activated Protein Kinase KinasesMutationProtein Bindingras ProteinsTransfectionMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Mitogen-Activated Protein Kinase Kinasesras Proteins

Identifiers

PMID16805921
PMCPMC1781522
OpenAlexW2116762319

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.