Identification of the Drosophila and Tribolium receptors for the recently discovered insect RYamide neuropeptides
Identification of the Drosophila and Tribolium receptors for the recently discovered insect RYamide neuropeptides
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DOI：
10.1016/j.bbrc.2011.07.131
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发表时间：
2011-09-09
影响因子：
3.1
通讯作者：
Grimmelikhuijzen, Cornelis J. P.
中科院分区：
文献类型：
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作者：
Collin, Caitlin;Hauser, Frank;Grimmelikhuijzen, Cornelis J. P.
一年前，我们发现了一个新的昆虫RYamide神经肽家族，其具有C-末端共有序列FFXXXRYamide，并且广泛存在于大多数昆虫中，包括果蝇Drosophila melanogaster和红粉甲虫Tribolium castaneum（F.豪瑟等人，9（2010）5296-5310）。在这里，我们确定了果蝇G蛋白偶联受体（GPCR）编码的基因CG 5811和其赤拟谷盗GPCR直系同源物作为昆虫RYamide受体。果蝇RYamide受体同样被两种果蝇RYamide神经肽激活（EC 50，1 × 10（-9）M）：RYamide-1（PVFFVASRYamide）和RYamide-2（NEHFFLGSRYamide），两者都包含在由基因CG 40733编码的前激素原中。赤拟谷盗受体对赤拟谷盗RYamide-2（ADAFFLGPRYamide; EC 50，5 × 10（-9）M）的亲和力略高于对赤拟谷盗RYamide-1（VQNLATFKTMMRYamide; EC 50，7 × 10（-8）M）的亲和力，这可能是由于最后一个肽不完全遵循RYamide共有序列规则的事实。昆虫中还有其他具有类似C-末端序列的神经肽（RWamide或RFamide），如FMRFamide、磺胺激肽、肌抑制素、神经肽F和各种短神经肽F。令人惊讶的是，这些神经肽对赤拟谷盗RYamide受体没有交叉反应性，而果蝇RYamide受体仅被高浓度（>10（-6）M）的神经肽F和短神经肽F-1非常轻微地激活，表明这两种RYamide受体对昆虫RYamide的激活非常特异，并且有效的昆虫RYamide受体激活需要序列FFXXXRYamide。系统发育树分析和其他氨基酸序列比较表明，昆虫RYamide受体与任何其他已知的昆虫或无脊椎动物/脊椎动物受体，包括哺乳动物神经肽Y和昆虫神经肽F和短神经肽F受体没有密切关系。发表在Flybase（www.flybase.org）上的基因表达数据显示，果蝇CG 5811基因在成年果蝇的后肠中显著表达，表明昆虫RYamides在消化或水重吸收中的作用。(C)2011 Elsevier Inc. All rights reserved.
One year ago, we discovered a new family of insect RYamide neuropeptides, which has the C-terminal consensus sequence FFXXXRYamide, and which is widely occurring in most insects, including the fruitfly Drosophila melanogaster and the red flour beetle Tribolium castaneum (F. Hauser et al., J. Proteome Res. 9 (2010) 5296-5310). Here, we identify a Drosophila G-protein-coupled receptor (GPCR) coded for by gene CG5811 and its Tribolium GPCR ortholog as insect RYamide receptors. The Drosophila RYamide receptor is equally well activated (EC50, 1 x 10(-9) M) by the two Drosophila RYamide neuropeptides: RYamide-1 (PVFFVASRYamide) and RYamide-2 (NEHFFLGSRYamide), both contained in a preprohormone coded for by gene CG40733. The Tribolium receptor shows a somewhat higher affinity to Tribolium RYamide-2 (ADAFFLGPRYamide; EC50, 5 x 10(-9) M) than to Tribolium RYamide-1 (VQNLATFKTMMRYamide; EC50, 7 x 10(-8) M), which might be due to the fact that the last peptide does not completely follow the RYamide consensus sequence rule. There are other neuropeptides in insects that have similar C-terminal sequences (RWamide or RFamide), such as the FMRFamides, sulfakinins, myosuppressins, neuropeptides F, and the various short neuropeptides F. Amazingly, these neuropeptides show no cross-reactivity to the Tribolium RYamide receptor, while the Drosophila RYamide receptor is only very slightly activated by high concentrations (>10(-6) M) of neuropeptide F and short neuropeptide F-1, showing that the two RYamide receptors are quite specific for activation by insect RYamides, and that the sequence FFXXXRYamide is needed for effective insect RYamide receptor activation. Phylogenetic tree analyses and other amino acid sequence comparisons show that the insect RYamide receptors are not closely related to any other known insect or invertebrate/vertebrate receptors, including mammalian neuropeptide Y and insect neuropeptide F and short neuropeptide F receptors. Gene expression data published in Flybase (www.flybase.org) show that the Drosophila CG5811 gene is significantly expressed in the hindgut of adult flies, suggesting a role of insect RYamides in digestion or water reabsorption. (C) 2011 Elsevier Inc. All rights reserved.