Beta-arrestin2 enhances beta2-adrenergic receptor-mediated nuclear translocation of ERK.

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Kobayashi H, Narita Y, Nishida M, Kurose H

Beta-arrestin2 enhances beta2-adrenergic receptor-mediated nuclear translocation of ERK.

Cell Signal. 2005 Oct;17(10):1248-53. Epub 2005 Feb 12.

PubMed ID

16038799 [ View in PubMed

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Abstract

Beta-arrestin mediates desensitization and internalization of beta-adrenergic receptors (betaARs), but also acts as a scaffold protein in extracellular signal-regulated kinase (ERK) cascade. Thus, we have examined the role of beta-arrestin2 in the betaAR-mediated ERK signaling pathways. Isoproterenol stimulation equally activated cytoplasmic and nuclear ERK in COS-7 cells expressing beta1AR or beta2AR. However, the activity of nuclear ERK was enhanced by co-expression of beta-arrestin2 in beta2AR-but not beta1AR-expressing cells. Pertussis toxin treatment and blockade of Gbetagamma action inhibited beta-arrestin2-enhanced nuclear activation of ERK, suggesting that beta-arrestin2 promotes nuclear ERK localization in a Gbetagamma dependent mechanism upon receptor stimulation. beta2AR containing the carboxyl terminal region of beta1AR lost the beta-arrestin2-promoted nuclear translocation. As the carboxyl terminal region is important for beta-arrestin binding, these results demonstrate that recruitment of beta-arrestin2 to carboxyl terminal region of beta2AR is important for ERK localization to the nucleus.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Isoprenaline	Beta-1 adrenergic receptor	Protein	Humans	Yes	Agonist	Details