Evidence map›Paper›PMID 30338897›Full record

ArticleChembiochem : a European journal of chemical biology2019

Interrogating PP1 Activity in the MAPK Pathway with Optimized PP1-Disrupting Peptides.

Yansong Wang, Bernhard Hoermann, Karolina Pavic, Malgorzata Trebacz, Pablo Rios, Maja Köhn

Open access · hybridAbstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2019. 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
0.6field-weighted citation impact, top 31% 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, 19 citations in OpenAlex.

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  12. Interrogating PP1 Activity in the MAPK Pathway with Optimized PP1-Disrupting Peptides.Chembiochem : a European journal of chemical biology · 2019
    Article
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 2 countries.

Yansong WangGenome Biology Unit, European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117, Heidelberg, Germany.
Bernhard HoermannGenome Biology Unit, European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117, Heidelberg, Germany.
Karolina PavicGenome Biology Unit, European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117, Heidelberg, Germany.
Malgorzata TrebaczFaculty of Biology and BIOSS-Centre for Biological Signalling Studies, Albert-Ludwigs-University of Freiburg, Schänzlestrasse 18, 79104, Freiburg, Germany.
Pablo RiosFaculty of Biology and BIOSS-Centre for Biological Signalling Studies, Albert-Ludwigs-University of Freiburg, Schänzlestrasse 18, 79104, Freiburg, Germany.
Maja KöhnGenome Biology Unit, European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117, Heidelberg, Germany.ORCID 0000-0001-8142-3504
University of Freiburg · DEEuropean Molecular Biology Laboratory · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein phosphatase-1 (PP1)-disrupting peptides (PDPs) are selective chemical modulators of PP1 that liberate the active PP1 catalytic subunit from regulatory proteins; thus allowing the dephosphorylation of nearby substrates. We have optimized the original cell-active PDP3 for enhanced stability, and obtained insights into the chemical requirements for stabilizing this 23-mer peptide for cellular applications. The optimized PDP-Nal was used to dissect the involvement of PP1 in the MAPK signaling cascade. Specifically, we have demonstrated that, in human osteosarcoma (U2OS) cells, phosphoMEK1/2 is a direct substrate of PP1, whereas dephosphorylation of phosphoERK1/2 is indirect and likely mediated through enhanced tyrosine phosphatase activity after PDP-mediated PP1 activation. Thus, as liberators of PP1 activity, PDPs represent a valuable tool for identifying the substrates of PP1 and understanding its role in diverse signaling cascades.

Indexed as

Amino Acid SequenceCell Line, TumorHistonesHumansMAP Kinase Kinase 1MAP Kinase Kinase Kinase 2MAP Kinase Signaling SystemMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3PeptidesPhosphorylationProtein Phosphatase 1HistonesMAP Kinase Kinase 1MAP Kinase Kinase Kinase 2Mitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3PeptidesProtein Phosphatase 1activatorsamino acidskinasespeptidesphosphorylation

Identifiers

PMID30338897
PMCPMC6471087
OpenAlexW2897191183

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.