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Top left: Comparison of polar core and three-element interactions between the inactive and intermediate conformations of βarr2. The ribbon diagram of βarr2 is colored dark gray. C7pp2 and the C-tail of βarr2IM are shown in pink and green, respectively. Hydrogen bonds stabilizing the polar core interactions are shown as dashed lines. Top right: CXCL12-induced trafficking of βarr2 as monitored using confocal microscopy in HEK293 cells expressing CXCR7WT and CXCR7E358A. The “Surface” images depict βarr2 localization at the plasma membrane shortly after agonist stimulation, representing initial recruitment of βarr2 to CXCR7. The “Endosomal” images show intracellular βarr2 localization at later time points, indicating receptor internalization. Scale bar is 10 μm. Bottom: Proposed arginine switch model for βarr2 activation by the CXCR7 Rp-tail. In the inactive state, Arg394, which we name as an “arginine switch,” is an integral component of the polar core, facilitating interaction. Simultaneously, the βarr2 C-tail engages with the N-domain through a 3E interaction. Upon C7pp2 binding to βarr2, the arginine switch undergoes rotation and forms a direct interaction with Glu358 of C7pp2, leading to partial disruption of the polar core. This stage represents an intermediate state preceding βarr2 activation, where the 3E interaction remains intact. Phosphorylation of Ser360/Thr361 further contributes to the disruption of the 3E interaction, triggering the release of the βarr2 C-tail, ultimately leading to the activation of βarr2.
β-arrestins regulate #GPCR signaling & trafficking, adopting multiple conformational states with different outcomes. This study shows how receptor CXCR7 induces stepwise conformational changes in β- #arrestin 2, uncovering an arginine switch mechanism of activation @plosbiology.org 🧪 plos.io/3UfTd71
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Top left: Comparison of polar core and three-element interactions between the inactive and intermediate conformations of βarr2. The ribbon diagram of βarr2 is colored dark gray. C7pp2 and the C-tail of βarr2IM are shown in pink and green, respectively. Hydrogen bonds stabilizing the polar core interactions are shown as dashed lines. Top right: CXCL12-induced trafficking of βarr2 as monitored using confocal microscopy in HEK293 cells expressing CXCR7WT and CXCR7E358A. The “Surface” images depict βarr2 localization at the plasma membrane shortly after agonist stimulation, representing initial recruitment of βarr2 to CXCR7. The “Endosomal” images show intracellular βarr2 localization at later time points, indicating receptor internalization. Scale bar is 10 μm. Bottom: Proposed arginine switch model for βarr2 activation by the CXCR7 Rp-tail. In the inactive state, Arg394, which we name as an “arginine switch,” is an integral component of the polar core, facilitating interaction. Simultaneously, the βarr2 C-tail engages with the N-domain through a 3E interaction. Upon C7pp2 binding to βarr2, the arginine switch undergoes rotation and forms a direct interaction with Glu358 of C7pp2, leading to partial disruption of the polar core. This stage represents an intermediate state preceding βarr2 activation, where the 3E interaction remains intact. Phosphorylation of Ser360/Thr361 further contributes to the disruption of the 3E interaction, triggering the release of the βarr2 C-tail, ultimately leading to the activation of βarr2.
β-arrestins regulate #GPCR signaling & trafficking, adopting multiple conformational states with different outcomes. This study shows how receptor CXCR7 induces stepwise conformational changes in β- #arrestin 2, uncovering an arginine switch mechanism of activation @plosbiology.org 🧪 plos.io/3UfTd71
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Top left: Comparison of polar core and three-element interactions between the inactive and intermediate conformations of βarr2. The ribbon diagram of βarr2 is colored dark gray. C7pp2 and the C-tail of βarr2IM are shown in pink and green, respectively. Hydrogen bonds stabilizing the polar core interactions are shown as dashed lines. Top right: CXCL12-induced trafficking of βarr2 as monitored using confocal microscopy in HEK293 cells expressing CXCR7WT and CXCR7E358A. The “Surface” images depict βarr2 localization at the plasma membrane shortly after agonist stimulation, representing initial recruitment of βarr2 to CXCR7. The “Endosomal” images show intracellular βarr2 localization at later time points, indicating receptor internalization. Scale bar is 10 μm. Bottom: Proposed arginine switch model for βarr2 activation by the CXCR7 Rp-tail. In the inactive state, Arg394, which we name as an “arginine switch,” is an integral component of the polar core, facilitating interaction. Simultaneously, the βarr2 C-tail engages with the N-domain through a 3E interaction. Upon C7pp2 binding to βarr2, the arginine switch undergoes rotation and forms a direct interaction with Glu358 of C7pp2, leading to partial disruption of the polar core. This stage represents an intermediate state preceding βarr2 activation, where the 3E interaction remains intact. Phosphorylation of Ser360/Thr361 further contributes to the disruption of the 3E interaction, triggering the release of the βarr2 C-tail, ultimately leading to the activation of βarr2.
β-arrestins regulate #GPCR signaling & trafficking, adopting multiple conformational states with different outcomes. This study shows how receptor CXCR7 induces stepwise conformational changes in β- #arrestin 2, uncovering an arginine switch mechanism of activation @plosbiology.org 🧪 plos.io/3UfTd71
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Eurofins Discoverx PathHunter eXpress GPR182 CHO-K1 β-Arrestin Orphan GPCR Assay, 2-Plate Kit. (93-0754E2CP1M) 930754E2CP1M @EurofinsKSA #Discoverx #PathHunter #eXpress #GPR182 #Arrestin #Orphan #930754E2CP1M
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