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

Hiroyuki Kobayashi, Yusuke Narita, Motohiro Nishida, Hitoshi Kurose

研究成果: ジャーナルへの寄稿記事

32 引用 (Scopus)

抜粋

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.

元の言語英語
ページ(範囲)1248-1253
ページ数6
ジャーナルCellular Signalling
17
発行部数10
DOI
出版物ステータス出版済み - 10 1 2005

    フィンガープリント

All Science Journal Classification (ASJC) codes

  • Cell Biology

これを引用