β-Arrestin 2:: A receptor-regulated MAPK scaffold for the activation of JNK3

被引:618
作者
McDonald, PH
Chow, CW
Miller, WE
Laporte, SA
Field, ME
Lin, FT
Davis, RJ
Lefkowitz, RJ
机构
[1] Duke Univ, Med Ctr, Howard Hughes Med Inst, Durham, NC 27710 USA
[2] Duke Univ, Med Ctr, Dept Med, Durham, NC 27710 USA
[3] Duke Univ, Med Ctr, Dept Cardiol, Durham, NC 27710 USA
[4] Duke Univ, Med Ctr, Dept Biochem, Durham, NC 27710 USA
[5] Univ Massachusetts, Sch Med, Dept Biochem & Mol Biol, Howard Hughes Med Inst, Worcester, MA 01605 USA
[6] Univ Massachusetts, Sch Med, Dept Biochem & Mol Biol, Program Mol Med, Worcester, MA 01605 USA
[7] Duke Univ, Med Ctr, Dept Cell Biol, Durham, NC 27710 USA
关键词
D O I
10.1126/science.290.5496.1574
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
beta -Arrestins, originally discovered in the context of heterotrimeric guanine nucleotide binding protein-coupled receptor (GPCR) desensitization, also function in internalization and signaling of these receptors. We identified c-Jun amino-terminal kinase 3 (JNK3) as a binding partner of beta -arrestin 2 using a yeast two-hybrid screen and by coimmunoprecipitation from mouse brain extracts or cotransfected COS-7 cells. The upstream JNK activators apoptosis signal-regulating kinase 1 (ASK1) and mitogen-activated protein kinase (MAPK) kinase 4 were also found in complex with beta -arrestin 2. cellular transfection of beta -arrestin 2 caused cytosolic retention of JNK3 and enhanced JNK3 phosphorylation stimulated by ASK1. Moreover, stimulation of the angiotensin II type 1A receptor activated JNK3 and triggered the colocalization of beta -arrestin 2 and active JNK3 to intracellular vesicles. Thus, beta -arrestin 2 acts as a scaffold protein, which brings the spatial distribution and activity of this MAPK module under the control of a GPCR.
引用
收藏
页码:1574 / 1577
页数:4
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