Beta‐2 adrenergic receptor mediated ERK activation is regulated by interaction with MAGI‐3
Beta‐2 adrenergic receptor mediated ERK activation is regulated by interaction with MAGI‐3
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DOI：
10.1016/j.febslet.2010.03.039
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发表时间：
2010-06
期刊：
影响因子：
3.5
通讯作者：
Xiaomei Yang;Junfang Zheng;Ying Xiong;Hui Shen;Licui Sun;Y. Huang;Chaoyuan Sun;Yang Li;Junqi He
中科院分区：
文献类型：
--
作者：
Xiaomei Yang;Junfang Zheng;Ying Xiong;Hui Shen;Licui Sun;Y. Huang;Chaoyuan Sun;Yang Li;Junqi He
β -2肾上腺素能受体（β2AR）具有一个羧基末端基序，可以与PSD-95/discs-large/ZO1同源（PDZ）结构域蛋白相互作用。在本文中，我们鉴定了膜相关鸟苷酸激酶倒置-3 （MAGI-3）作为β2AR的一个新的结合伙伴。β2AR的羧基末端与MAGI-3的第五个PDZ结构域具有高亲和力，受体的最后四个氨基酸（D-S-L-L）是相互作用的关键决定因素。在细胞中，全长β2AR与MAGI-3的关联是组成性的，并通过受体的激动剂刺激而增强。我们的数据还表明，β 2ar刺激的细胞外信号调节激酶1/2 （ERK1/2）的激活被MAGI-3的表达大大延缓。这些数据表明，MAGI-3通过β2AR和MAGI-3之间的物理相互作用调节β2AR介导的ERK激活。结构摘要：MINT-7716556: beta2AR （uniprotkb:P07550）通过抗标签共免疫沉淀（MI:0007）与MAGI-3 （uniprotkb:Q5TCQ9）物理相互作用（MI:0915） MINT-7716593: beta2AR （uniprotkb:P18762）通过抗诱饵共免疫沉淀（MI:0006）与MAGI-3 （uniprotkb:Q9EQJ9）物理相互作用（MI:0915） MINT-7716630: MAGI-3 （uniprotkb:Q5TCQ9）和beta2AR （uniprotkb:P07550）共定位（MI:0403）通过荧光显微镜（MI:0416） MINT-7716382, MINT-7716335：MAGI-3 （uniprotkb:Q5TCQ9）通过下拉（MI:0096）与beta2AR （uniprotkb:P07550）物理相互作用（MI:0915） MINT-7716320, MINT-7716422, MINT-7716502, MINT-7716450, MINT-7716470: beta2AR （uniprotkb:P07550）通过下拉（MI:0096）与MAGI-3 （uniprotkb:Q5TCQ9）结合（MI:0407）
The beta-2 adrenergic receptor (β2AR) has a carboxyl terminus motif that can interact with PSD-95/discs-large/ZO1 homology (PDZ) domain-containing proteins. In this paper, we identified membrane-associated guanylate kinase inverted-3 (MAGI-3) as a novel binding partner of β2AR. The carboxyl terminus of β2AR binds with high affinity to the fifth PDZ domain of MAGI-3, with the last four amino acids (D-S-L-L) of the receptor being the key determinants of the interaction. In cells, the association of full-length β2AR with MAGI-3 occurs constitutively and is enhanced by agonist stimulation of the receptor. Our data also demonstrated that β2AR-stimulated extracellular signal-regulated kinase-1/2 (ERK1/2) activation was substantially retarded by MAGI-3 expression. These data suggest that MAGI-3 regulates β2AR-mediated ERK activation through the physical interaction between β2AR and MAGI-3. STRUCTURED SUMMARY: MINT-7716556: beta2AR (uniprotkb:P07550) physically interacts (MI:0915) with MAGI-3 (uniprotkb:Q5TCQ9) by anti tag coimmunoprecipitation (MI:0007) MINT-7716593: beta2AR (uniprotkb:P18762) physically interacts (MI:0915) with MAGI-3 (uniprotkb:Q9EQJ9) by anti bait coimmunoprecipitation (MI:0006) MINT-7716630: MAGI-3 (uniprotkb:Q5TCQ9) and beta2AR (uniprotkb:P07550) colocalize (MI:0403) by fluorescence microscopy (MI:0416) MINT-7716382, MINT-7716335: MAGI-3 (uniprotkb:Q5TCQ9) physically interacts (MI:0915) with beta2AR (uniprotkb:P07550) by pull down (MI:0096) MINT-7716320, MINT-7716422, MINT-7716502, MINT-7716450, MINT-7716470: beta2AR (uniprotkb:P07550) binds (MI:0407) to MAGI-3 (uniprotkb:Q5TCQ9) by pull down (MI:0096)