Evidence map›Paper›PMID 27247265›Full record

ArticleMolecular and cellular biology2016

ZDHHC3 Tyrosine Phosphorylation Regulates Neural Cell Adhesion Molecule Palmitoylation.

Patricia Marie-Jeanne Lievens, Tatiana Kuznetsova, Gaga Kochlamazashvili, Fabrizia Cesca, Natalya Gorinski, Dalia Abdel Galil, Volodimir Cherkas, Natalia Ronkina, Juri Lafera, Matthias Gaestel and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

26 citing papers in PubMed, 40 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. DHHC17 Is a New Regulator of AMPK Signaling.Molecular and cellular biology · 2022
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  7. Review
  8. Insights into auto-RSC chemical biology · 2021
    Review
  9. Protein S-Palmitoylation and Lung Diseases.Advances in experimental medicine and biology · 2021
    Article
  10. Regulation of Dynamic Protein S-Acylation.Frontiers in molecular biosciences · 2021
    Review
  11. Review
  12. Regulatory effects of post-translational modifications on zDHHCThe Journal of biological chemistry · 2020
    Review
  13. The Journal of biological chemistry · 2020
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. 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

12 authors at 4 institutions in 3 countries.

Patricia Marie-Jeanne LievensDepartment of Neuroscience and Brain Technologies, Istituto Italiano di Tecnologia, Genoa, Italy Department of Neurosciences, Biomedicine and Movement Sciences, Section of Biology and Genetics, University of Verona, Verona, Italy.
Tatiana KuznetsovaDepartment of Neuroscience and Brain Technologies, Istituto Italiano di Tecnologia, Genoa, Italy St. Petersburg State University, St. Petersburg, Russia.
Gaga KochlamazashviliDepartment of Neuroscience and Brain Technologies, Istituto Italiano di Tecnologia, Genoa, Italy.
Fabrizia CescaDepartment of Neuroscience and Brain Technologies, Istituto Italiano di Tecnologia, Genoa, Italy.
Natalya GorinskiDepartment of Cellular Neurophysiology, Hannover Medical School, Hannover, Germany.
Dalia Abdel GalilDepartment of Cellular Neurophysiology, Hannover Medical School, Hannover, Germany.
Volodimir CherkasDepartment of Cellular Neurophysiology, Hannover Medical School, Hannover, Germany.
Natalia RonkinaDepartment of Physiological Chemistry, Hannover Medical School, Hannover, Germany.
Juri LaferaDepartment of Physiological Chemistry, Hannover Medical School, Hannover, Germany.
Matthias GaestelDepartment of Physiological Chemistry, Hannover Medical School, Hannover, Germany.
Evgeni PonimaskinDepartment of Cellular Neurophysiology, Hannover Medical School, Hannover, Germany ponimaskin.evgeni@mh-hannover.de alexander.dityatev@dzne.de.
Alexander DityatevDepartment of Neuroscience and Brain Technologies, Istituto Italiano di Tecnologia, Genoa, Italy Molecular Neuroplasticity Group, DZNE, Magdeburg, Germany Medical Faculty, Otto von Guericke University, Magdeburg, Germany Center for Behavioral Brain Sciences (CBBS), Magdeburg, Germany ponimaskin.evgeni@mh-hannover.de alexander.dityatev@dzne.de.ORCID 0000-0002-0472-0553
Medizinische Hochschule Hannover · DEItalian Institute of Technology · ITSt Petersburg University · RUUniversity of Verona · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The neural cell adhesion molecule (NCAM) mediates cell-cell and cell-matrix adhesion. It is broadly expressed in the nervous system and regulates neurite outgrowth, synaptogenesis, and synaptic plasticity. Previous in vitro studies revealed that palmitoylation of NCAM is required for fibroblast growth factor 2 (FGF2)-stimulated neurite outgrowth and identified the zinc finger DHHC (Asp-His-His-Cys)-containing proteins ZDHHC3 and ZDHHC7 as specific NCAM-palmitoylating enzymes. Here, we verified that FGF2 controlled NCAM palmitoylation in vivo and investigated molecular mechanisms regulating NCAM palmitoylation by ZDHHC3. Experiments with overexpression and pharmacological inhibition of FGF receptor (FGFR) and Src revealed that these kinases control tyrosine phosphorylation of ZDHHC3 and that ZDHHC3 is phosphorylated by endogenously expressed FGFR and Src proteins. By site-directed mutagenesis, we found that Tyr18 is an FGFR1-specific ZDHHC3 phosphorylation site, while Tyr295 and Tyr297 are specifically phosphorylated by Src kinase in cell-based and cell-free assays. Abrogation of tyrosine phosphorylation increased ZDHHC3 autopalmitoylation, enhanced interaction with NCAM, and upregulated NCAM palmitoylation. Expression of ZDHHC3 with tyrosine mutated in cultured hippocampal neurons promoted neurite outgrowth. Our findings for the first time highlight that FGFR- and Src-mediated tyrosine phosphorylation of ZDHHC3 modulates ZDHHC3 enzymatic activity and plays a role in neuronal morphogenesis.

Indexed as

AcyltransferasesAnimalsCells, CulturedFibroblast Growth Factor 2Gene Expression RegulationLipoylationMembrane ProteinsMiceMutationNeural Cell Adhesion MoleculesNeuritesPhosphorylationReceptors, Fibroblast Growth Factorsrc-Family KinasesTyrosineAcyltransferasesFibroblast Growth Factor 2GODZ protein, mouseMembrane ProteinsNeural Cell Adhesion MoleculesReceptors, Fibroblast Growth Factorsrc-Family KinasesTyrosine

Identifiers

PMID27247265
PMCPMC4985929
OpenAlexW2518360974

What OpenQuestion holds

Textmetadata
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Registered trials

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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.