Evidence map›Paper›PMID 32471307›Full record

ReviewInternational journal of molecular sciences2020

Phosphorylation Sites in Protein Kinases and Phosphatases Regulated by Formyl Peptide Receptor 2 Signaling.

Maria Carmela Annunziata, Melania Parisi, Gabriella Esposito, Gabriella Fabbrocini, Rosario Ammendola, Fabio Cattaneo

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

22 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. NOX Dependent ROS Generation and Cell Metabolism.International journal of molecular sciences · 2023
    Review
  13. Review
  14. Article
  15. Crystal structure of the phosphorylatedActa biochimica et biophysica Sinica · 2022
    Article
  16. Article
  17. Article
  18. Review
  19. Caulerpin MitigatesInternational journal of molecular sciences · 2021
    Article
  20. Review
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.

Maria Carmela AnnunziataDepartment of Clinical Medicine and Surgery, University of Naples Federico II, School of Medicine, Via S. Pansini 5, 80131 Naples, Italy.
Melania ParisiDepartment of Clinical Medicine and Surgery, University of Naples Federico II, School of Medicine, Via S. Pansini 5, 80131 Naples, Italy.
Gabriella EspositoDepartment of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, School of Medicine, Via S. Pansini 5, 80131 Naples, Italy.ORCID 0000-0002-4255-7312
Gabriella FabbrociniDepartment of Clinical Medicine and Surgery, University of Naples Federico II, School of Medicine, Via S. Pansini 5, 80131 Naples, Italy.
Rosario AmmendolaDepartment of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, School of Medicine, Via S. Pansini 5, 80131 Naples, Italy.ORCID 0000-0003-1655-8028
Fabio CattaneoDepartment of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, School of Medicine, Via S. Pansini 5, 80131 Naples, Italy.ORCID 0000-0002-5833-8333
University of Naples Federico II · IT

Funding

Sviluppo di Approcci Terapeutici INnovativi per patologie neoplastiche resistenti ai trattamenti (SATIN) CUP B61C17000070007 - SURF 17061BP000000002
6 · The paper itself

Abstract

FPR1, FPR2, and FPR3 are members of Formyl Peptides Receptors (FPRs) family belonging to the GPCR superfamily. FPR2 is a low affinity receptor for formyl peptides and it is considered the most promiscuous member of this family. Intracellular signaling cascades triggered by FPRs include the activation of different protein kinases and phosphatase, as well as tyrosine kinase receptors transactivation. Protein kinases and phosphatases act coordinately and any impairment of their activation or regulation represents one of the most common causes of several human diseases. Several phospho-sites has been identified in protein kinases and phosphatases, whose role may be to expand the repertoire of molecular mechanisms of regulation or may be necessary for fine-tuning of switch properties. We previously performed a phospho-proteomic analysis in FPR2-stimulated cells that revealed, among other things, not yet identified phospho-sites on six protein kinases and one protein phosphatase. Herein, we discuss on the selective phosphorylation of Serine/Threonine-protein kinase N2, Serine/Threonine-protein kinase PRP4 homolog, Serine/Threonine-protein kinase MARK2, Serine/Threonine-protein kinase PAK4, Serine/Threonine-protein kinase 10, Dual specificity mitogen-activated protein kinase kinase 2, and Protein phosphatase 1 regulatory subunit 14A, triggered by FPR2 stimulation. We also describe the putative FPR2-dependent signaling cascades upstream to these specific phospho-sites.

Indexed as

Signal TransductionAmino Acid MotifsAnimalsHumansPhosphoprotein PhosphatasesPhosphorylationProtein Processing, Post-TranslationalProtein Serine-Threonine KinasesReceptors, Formyl PeptidePhosphoprotein PhosphatasesProtein Serine-Threonine KinasesReceptors, Formyl Peptidecell signalingFPR2MAP2K2MARK2PAK4phospho-sitesPKN2PPP1R14A.PRP4STK10

Identifiers

PMID32471307
PMCPMC7312799
OpenAlexW3032771029

What Socratic 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 Socratic graph.