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Article Dans Une Revue Molecular Pharmacology Année : 2019

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

Résumé

The C-X-C motif 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 subcellular 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 states. 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 light on their regulation and pathophysiological functions.
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Dates et versions

hal-02364301 , version 1 (29-11-2020)

Identifiants

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Amos Fumagalli, Aurelien Zarca, Maria Neves, Birgit Caspar, Stephen Hill, et al.. CXCR4/ACKR3 phosphorylation and recruitment of interacting proteins: key mechanisms regulating their functional status. Molecular Pharmacology, 2019, 96, pp.mol.118.115360. ⟨10.1124/mol.118.115360⟩. ⟨hal-02364301⟩
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