β-Arrestin2 enhances β2-adrenergic receptor-mediated nuclear translocation of ERK

Hiroyuki Kobayashi, Yusuke Narita, Motohiro Nishida, Hitoshi Kurose

Research output: Contribution to journalArticle

32 Citations (Scopus)

Abstract

β-Arrestin mediates desensitization and internalization of β-adrenergic receptors (βARs), but also acts as a scaffold protein in extracellular signal-regulated kinase (ERK) cascade. Thus, we have examined the role of β-arrestin2 in the βAR-mediated ERK signaling pathways. Isoproterenol stimulation equally activated cytoplasmic and nuclear ERK in COS-7 cells expressing β1AR or β2AR. However, the activity of nuclear ERK was enhanced by co-expression of β-arrestin2 in β2AR-but not β1AR-expressing cells. Pertussis toxin treatment and blockade of Gβγ action inhibited β-arrestin2-enhanced nuclear activation of ERK, suggesting that β-arrestin2 promotes nuclear ERK localization in a Gβγ dependent mechanism upon receptor stimulation. β2AR containing the carboxyl terminal region of β1AR lost the β-arrestin2- promoted nuclear translocation. As the carboxyl terminal region is important for β-arrestin binding, these results demonstrate that recruitment of β-arrestin2 to carboxyl terminal region of β2AR is important for ERK localization to the nucleus.

Original languageEnglish
Pages (from-to)1248-1253
Number of pages6
JournalCellular Signalling
Volume17
Issue number10
DOIs
Publication statusPublished - Oct 1 2005

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Extracellular Signal-Regulated MAP Kinases
Adrenergic Receptors
Arrestin
COS Cells
Pertussis Toxin
Isoproterenol
Proteins

All Science Journal Classification (ASJC) codes

  • Cell Biology

Cite this

β-Arrestin2 enhances β2-adrenergic receptor-mediated nuclear translocation of ERK. / Kobayashi, Hiroyuki; Narita, Yusuke; Nishida, Motohiro; Kurose, Hitoshi.

In: Cellular Signalling, Vol. 17, No. 10, 01.10.2005, p. 1248-1253.

Research output: Contribution to journalArticle

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