Neuropeptide GPCRs in C. elegans.
Neuropeptide GPCRs in C. elegans.
复制标题
DOI：
10.3389/fendo.2012.00167
复制
发表时间：
2012
影响因子：
5.2
通讯作者：
Schoofs L
中科院分区：
文献类型：
--
作者：
Frooninckx L;Van Rompay L;Temmerman L;Van Sinay E;Beets I;Janssen T;Husson SJ;Schoofs L
与大多数生物体一样，线虫秀丽隐杆线虫严重依赖神经肽能信号传导。由于强大的分子和遗传工具的可用性，这种微小的动物代表了一个合适的模型系统，可以用单细胞分辨率研究神经肽能信号网络。蠕虫完整基因组序列的可用性使研究人员能够浏览它，发现假定的神经肽及其同源 G 蛋白偶联受体 (GPCR)。人们对线虫神经肽 GPCR 的数量做出了许多预测。在这篇综述中，我们报告了经过验证和预测的秀丽隐杆线虫神经肽 GPCR 的最新技术。根据预测的神经肽 GPCR 与昆虫和脊椎动物中的直系同源 GPCR 的相似性，将其纳入受体分类系统。为每个预测的神经肽 GPCR（受体去孤儿化）指定天然配体是表征过程中的关键步骤。去孤儿化策略的发展导致人们对秀丽隐杆线虫神经肽能信号传导的了解显着增加。补充定位和功能研究表明，神经肽及其 GPCR 代表了秀丽隐杆线虫行为变异的丰富潜在来源。在这里，我们回顾了迄今为止在秀丽隐杆线虫中进行功能表征的所有神经肽能信号通路。
Like most organisms, the nematode Caenorhabditis elegans relies heavily on neuropeptidergic signaling. This tiny animal represents a suitable model system to study neuropeptidergic signaling networks with single cell resolution due to the availability of powerful molecular and genetic tools. The availability of the worm’s complete genome sequence allows researchers to browse through it, uncovering putative neuropeptides and their cognate G protein-coupled receptors (GPCRs). Many predictions have been made about the number of C. elegans neuropeptide GPCRs. In this review, we report the state of the art of both verified as well as predicted C. elegans neuropeptide GPCRs. The predicted neuropeptide GPCRs are incorporated into the receptor classification system based on their resemblance to orthologous GPCRs in insects and vertebrates. Appointing the natural ligand(s) to each predicted neuropeptide GPCR (receptor deorphanization) is a crucial step during characterization. The development of deorphanization strategies resulted in a significant increase in the knowledge of neuropeptidergic signaling in C. elegans. Complementary localization and functional studies demonstrate that neuropeptides and their GPCRs represent a rich potential source of behavioral variability in C. elegans. Here, we review all neuropeptidergic signaling pathways that so far have been functionally characterized in C. elegans.