The neuronal Ca2+-binding protein 2 (NECAB2) interacts with the adenosine A2A receptor and modulates the cell surface expression and function of the receptor
The neuronal Ca2+-binding protein 2 (NECAB2) interacts with the adenosine A2A receptor and modulates the cell surface expression and function of the receptor
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DOI：
10.1016/j.mcn.2007.05.007
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发表时间：
2007-09-01
影响因子：
3.5
通讯作者：
Ciruela, Francisco
中科院分区：
文献类型：
--
作者：
Cancla, Laia;Lujan, Rafael;Ciruela, Francisco
七烷泛膜也被称为G蛋白偶联受体（GPCR）与多种细胞内蛋白相互作用，其功能是调节受体交通和/或信号传导。通过酵母双杂交筛选，发现神经元钙结合蛋白NECAB2是腺苷a （2A）受体（a (2A)R）的结合伙伴，与腺苷a （2A）受体的c端结构域相互作用。共定位、共免疫沉淀和下拉实验表明，A2AR和NECAB2在转染的HEK-293细胞和大鼠纹状体中均具有密切和特异性的相互作用。免疫电镜检测大鼠纹状体结构中的NECAB2和A2AR表明，这两种蛋白在相同的谷氨酸神经末梢共分布。NECAB2与A2AR的相互作用调节了细胞表面表达、配体依赖性内化和受体介导的MAPK通路激活。总的来说，这些结果表明A2AR与NECAB2在纹状体神经元中共同表达，并且相互作用与A(2A)R功能有关。(c) 2007爱思唯尔公司版权所有。
Heptaspanning membrane also known as G protein-coupled receptors (GPCR) do interact with a variety of intracellular proteins whose function is regulate receptor traffic and/or signaling. Using a yeast two-hybrid screen, NECAB2, a neuronal calcium binding protein, was identified as a binding partner for the adenosine A(2A) receptor (A(2A)R) interacting with its C-terminal domain. Co-localization, co-immunoprecipitation and pull-down experiments showed a close and specific interaction between A2AR and NECAB2 in both transfected HEK-293 cells and also in rat striatum. Immunoclectron microscopy detection of NECAB2 and A2AR in the rat striatopallidall structures indicated that both proteins are co-distributed in the same glutamatergic nerve terminals. The interaction of NECAB2 with A2AR modulated the cell surface expression, the ligand-dependent internalization and the receptor-mediated activation of the MAPK pathway. Overall, these results show that A2AR interacts with NECAB2 in striatal neurones co-expressing the two proteins and that the interaction is relevant for A(2A)R function. (c) 2007 Elsevier Inc. All rights reserved.