Proteins that smell: pheromone recognition and signal transduction.

Proteins that smell: pheromone recognition and signal transduction.
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DOI:
10.1016/0968-0896(96)00033-8
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发表时间:
1996-03
影响因子:
3.5
通讯作者:
G. Prestwich
G. Prestwich
中科院分区:
医学3区
文献类型:
--
作者:
G. Prestwich

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鳞翅目昆虫对信息素的感知需要蛾触角中配体特异性信息素结合蛋白(PBPs)对信息素分子的初始识别和转运,然后通过跨膜G蛋白偶联的气味受体蛋白识别配体或PBPs-配体复合物。该信号通过激活特异性磷脂酶C、胞内释放1,4,5-三磷酸肌醇(IP 3)和IP 3门控打开离子通道来转导。个体信息素特异性PBPs提供初始配体识别事件并编码配体特异性。我们已经使用光亲和标记,cDNA文库筛选和克隆,蛋白质表达,一种新的结合试验和定点突变来定义PBPs的配体特异性。
Pheromone perception in Lepidoptera requires initial recognition and transport of the pheromone molecule by ligand-specific pheromone binding proteins (PBPs) in the moth antennae, followed by recognition of the ligand or PBP-ligand complex by a transmembrane G-protein-coupled odorant receptor protein. This signal is transduced by activation of a specific phospholipase C, intracellular release of inositol 1,4,5-trisphosphate (IP3) and IP3-gated opening of an ion channel. Individual pheromone-specific PBPs provide the initial ligand recognition event and encode ligand specificity. We have used photoaffinity labeling, cDNA library screening and cloning, protein expression, a novel binding assay and site-directed mutagenesis to define the ligand specificity of PBPs.