β‐Arrestin is involved in the desensitization but not in the internalization of the somatostatin receptor 2A expressed in CHO cells

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Abstract
The interaction of β-arrestin-1 with the somatostatin receptor type 2A (sst2A) was monitored using both biochemical and confocal imaging approaches. We show that, using transient transfection of either β-arrestin-1 or its dominant negative Δ-arrestin-1 in CHO cells stably transfected with the sst2A, β-arrestin-1 is colocalized with the receptor in endosomal vesicles after somatostatin-induced sequestration. However, this interaction leads to a role of β-arrestin-1 in the desensitization of the sst2A rather than in the internalization process of the receptor–ligand complex