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Research ArticleMinireview

CXCR4/ACKR3 phosphorylation and recruitment of interacting proteins: key mechanisms regulating their functional status

Amos Fumagalli, Aurelien Zarca, Maria Neves, Birgit Caspar, Stephen J Hill, Federico Mayor, Martine J Smit and Philippe Marin
Molecular Pharmacology March 5, 2019, mol.118.115360; DOI: https://doi.org/10.1124/mol.118.115360
Amos Fumagalli
Institut de Genomique Fonctionnelle (CNRS);
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Aurelien Zarca
VU University of Amsterdam;
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Maria Neves
Universidad Autonoma Madrid;
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Birgit Caspar
University of Nottingham
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Stephen J Hill
University of Nottingham
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Federico Mayor
Universidad Autonoma Madrid;
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Martine J Smit
VU University of Amsterdam;
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Philippe Marin
Institut de Genomique Fonctionnelle (CNRS);
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Abstract

The C-X-C chemokine receptor type 4 (CXCR4) and the atypical chemokine receptor 3 (ACKR3/CXCR7) are class A G protein-coupled receptors (GPCRs). Accumulating evidence indicates that GPCR sub-cellular localization, trafficking, transduction properties and, ultimately, their pathophysiological functions are regulated by both interacting proteins and post-translational modifications. This has encouraged the development of novel techniques to characterize the GPCR interactome and to identify residues subjected to post-translational modifications, with a special focus on phosphorylation. This review first describes state-of-the-art methods for the identification of GPCR-interacting proteins and GPCR phosphorylated sites. In addition, we provide an overview of the current knowledge of CXCR4 and ACKR3 post-translational modifications and an exhaustive list of previously identified CXCR4 or ACKR3 interacting proteins. We then describe studies highlighting the importance of the reciprocal influence of CXCR4/ACKR3 interactomes and phosphorylation state. We also discuss their impact on the functional status of each receptor. These studies suggest that deeper knowledge of the CXCR4/ACKR3 interactomes along with their phosphorylation and ubiquitination status would shed new lights on their regulation and pathophysiological functions.

  • Chemokine receptors
  • G protein-coupled receptor kinases (GPKs)
  • G protein-coupled receptors (GPCRs)
  • Immunoprecipitation
  • Protein phosphorylation
  • Protein-protein interactions
  • Signal transduction networks
  • The American Society for Pharmacology and Experimental Therapeutics
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Molecular Pharmacology: 97 (1)
Molecular Pharmacology
Vol. 97, Issue 1
1 Jan 2020
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Research ArticleMinireview

CXCR4/ACKR3 phosphorylation and recruitment of interacting proteins: key mechanisms regulating their functional status

Amos Fumagalli, Aurelien Zarca, Maria Neves, Birgit Caspar, Stephen J Hill, Federico Mayor, Martine J Smit and Philippe Marin
Molecular Pharmacology March 5, 2019, mol.118.115360; DOI: https://doi.org/10.1124/mol.118.115360

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Research ArticleMinireview

CXCR4/ACKR3 phosphorylation and recruitment of interacting proteins: key mechanisms regulating their functional status

Amos Fumagalli, Aurelien Zarca, Maria Neves, Birgit Caspar, Stephen J Hill, Federico Mayor, Martine J Smit and Philippe Marin
Molecular Pharmacology March 5, 2019, mol.118.115360; DOI: https://doi.org/10.1124/mol.118.115360
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