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  • G-protein-coupled receptor phosphorylation: where, when and by whom
    This review investigates the possibility that the multi-site nature of GPCR phosphorylation reflects the importance of specific phosphorylation events which mediate distinct signalling outcomes In this way receptor phosphorylation may provide for a flexible regulatory mechanism that can be tailored in a tissue specific manner to regulate
  • How GPCR Phosphorylation Patterns Orchestrate Arrestin-Mediated . . .
    The number and arrangement of phosphates may vary substantially for a given GPCR, and different phosphorylation patterns trigger different arrestin-mediated effects Here, we determine how GPCR phosphorylation influences arrestin behavior by using atomic-level simulations and site-directed spectroscopy to reveal the effects of phosphorylation
  • Frontiers | Post-Translational Modifications of G Protein–Coupled . . .
    The crosstalk between GPCR phosphorylation and ubiquitination has been extensively studied For instance, mutation of phosphorylated residues S324 and S325 of CXCR4 inhibited agonist-induced ubiquitination of nearby lysine residues and eventually affected receptor degradation
  • How genetic errors in GPCRs affect their function . . . - ScienceDirect
    It appears that the majority of GPCR mutations exert their effects by causing general structural rearrangements in receptors, rather than by affecting key residues responsible for ligand or G protein interactions
  • Unintended Effects of GPCR-Targeted Drugs on the Cancer Phenotype
    Epidemiological and experimental evidence indicate that widely used GPCR-targeted drugs may promote or inhibit cancer progression It is crucial that we more fully understand the indirect effects of GPCR-targeted drugs on the cancer phenotype
  • Emerging Paradigms of G Protein-Coupled Receptor Dephosphorylation . . .
    For many GPCRs quenching of this signal involves phosphorylation of the receptor by GPCR kinases (GRKs) Phosphorylation by GRKs increases the affinity for arrestins, which uncouple the receptor from the G protein and target the receptor to clathrin-coated pits (CCPs) for internalization
  • Posttranslational modifications in GPCR internalization
    GPCR phosphorylation and palmitoylation have been reported to regulate the pit formation GPCR phosphorylation is known to create a negatively charged surface that facilitates the pit formation by increasing interaction between the receptor and AP-2 For example, upon thrombin stimulation, PAR1 can be phosphorylated at the distal C terminus
  • Phosphorylation-independent attenuation of GPCR signalling
    Second-messenger-dependent protein kinases (e g protein kinases A and C) are activated in response to GPCR-stimulated increases in intracellular second messengers and participate in GPCR signalling by mediating the phosphorylation of downstream target proteins
  • Physiological role of G-protein coupled receptor phosphorylation
    In this chapter, we address this issue by describing how GPCR phosphorylation might vary depending on the cell type in which the receptor is expressed and how this might be employed to drive selective regulation of physiological responses





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