Evidence map›Paper›PMID 33085143›Full record

ArticleChembiochem : a European journal of chemical biology2021

Towards Dissecting the Mechanism of Protein Phosphatase-1 Inhibition by Its C-Terminal Phosphorylation.

Francesca Salvi, Bernhard Hoermann, Javier Del Pino García, Miriam Fontanillo, Rita Derua, Monique Beullens, Mathieu Bollen, Orsolya Barabas, Maja Köhn

Open access · hybridAbstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

13 citing papers in PubMed, 19 citations in OpenAlex.

  1. Review
  2. Article
  3. LMTK2 switches on canonical TGF-β1 signaling in human bronchial epithelial cells.American journal of physiology. Lung cellular and molecular physiology · 2024
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Regulation of Synaptic Transmission and Plasticity by Protein Phosphatase 1.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
    Review
  12. Article
  13. 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

9 authors at 4 institutions in 2 countries.

Francesca SalviGenome Biology Unit, European Molecular Biology Laboratory, Meyerhofstraße 1, 69117, Heidelberg, Germany.ORCID 0000-0001-5294-1310
Bernhard HoermannSignalling Research Centres BIOSS and CIBSS, University of Freiburg, Schänzlestraße 18, 79104, Freiburg, Germany.ORCID 0000-0002-4014-0329
Javier Del Pino GarcíaLaboratory of Biosignaling and Therapeutics Department of Cellular and Molecular Medicine, KU Leuven, Herestraat 49, 3000, Leuven, Belgium.
Miriam FontanilloGenome Biology Unit, European Molecular Biology Laboratory, Meyerhofstraße 1, 69117, Heidelberg, Germany.
Rita DeruaLaboratory of Protein Phosphorylation and Proteomics Department of Cellular and Molecular Medicine, KU Leuven, Herestraat 49, 3000, Leuven, Belgium.
Monique BeullensLaboratory of Biosignaling and Therapeutics Department of Cellular and Molecular Medicine, KU Leuven, Herestraat 49, 3000, Leuven, Belgium.
Mathieu BollenLaboratory of Biosignaling and Therapeutics Department of Cellular and Molecular Medicine, KU Leuven, Herestraat 49, 3000, Leuven, Belgium.
Orsolya BarabasStructural and Computational Biology Unit, European Molecular Biology Laboratory, Meyerhofstraße 1, 69117, Heidelberg, Germany.ORCID 0000-0002-2873-5872
Maja KöhnGenome Biology Unit, European Molecular Biology Laboratory, Meyerhofstraße 1, 69117, Heidelberg, Germany.ORCID 0000-0001-8142-3504
KU Leuven · BEEuropean Molecular Biology Laboratory · DEUniversity of Freiburg · DEEuropean Molecular Biology Laboratory · DE

Funding

ERC Consolidator Grant 865119ERC Starting Grant 336567FWO grant G095119 N
6 · The paper itself

Abstract

Phosphoprotein phosphatase-1 (PP1) is a key player in the regulation of phospho-serine (pSer) and phospho-threonine (pThr) dephosphorylation and is involved in a large fraction of cellular signaling pathways. Aberrant activity of PP1 has been linked to many diseases, including cancer and heart failure. Besides a well-established activity control by regulatory proteins, an inhibitory function for phosphorylation (p) of a Thr residue in the C-terminal intrinsically disordered tail of PP1 has been demonstrated. The associated phenotype of cell-cycle arrest was repeatedly proposed to be due to autoinhibition of PP1 through either conformational changes or substrate competition. Here, we use PP1 variants created by mutations and protein semisynthesis to differentiate between these hypotheses. Our data support the hypothesis that pThr exerts its inhibitory function by mediating protein complex formation rather than by a direct mechanism of structural changes or substrate competition.

Indexed as

HumansIntracellular Signaling Peptides and ProteinsPhosphorylationProtein BindingProtein ConformationProtein DomainsProtein Phosphatase 1SerineThreonineIntracellular Signaling Peptides and ProteinsProtein Phosphatase 1protein phosphatase inhibitor-1SerineThreoninebiomimetic synthesispeptidesphosphorylationprotein phosphatase-1 (PP1) regulationprotein semisynthesis

Identifiers

PMID33085143
PMCPMC7984433
OpenAlexW3093856117

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.