IDENTIFICATION OF PROTEINS ASSOCIATED WITH NICOTINIC ACETYLCHOLINE RECEPTORS

该子项目是利用NIH/NCRR资助的中心赠款提供的资源的许多研究子项目之一。子项目和研究者（PI）可能从另一个NIH来源获得主要资金，因此可以在其他CRISP条目中表示。所列机构为中心，不一定是研究者所在机构。“一种来自秀丽隐杆线虫的烟碱乙酰胆碱受体，存在于肌肉和神经元中，已经被纯化到明显的同质性，包括辅助蛋白。甘油梯度离心后，这些额外的蛋白质与受体共沉淀为11 S复合物，证实了它们的紧密结合。据我们所知，这是第一次可以将烟碱受体与相关蛋白一起纯化。因此，它不仅对C。elegans社区，以确定这些蛋白质，其中一些可能参与调节烟碱受体的功能和/或表达。这应该是直截了当的，因为C。线虫基因组序列是已知的。利用RNA介导的干扰和反向遗传学在C. elegans系统"

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. "A nicotinic acetylcholine receptor from Caenorhabditis elegans, which is present in muscles and neurons, has been purified to apparent homogeneity, including accessory proteins. These additional proteins do co-sediment with the receptor as an 11 S complex upon glycerol gradient centrifugation, confirming their tight association. To our knowledge, this is the first time that nicotinic receptors could be purified together with associated proteins. It is thus of major interest, not only for the C. elegans community, to identify these proteins, some of which may be involved in regulating the function and/or expression of nicotinic receptors. This should be straightforward, since the C. elegans genome sequence is known. The functional characterization of these potentially novel proteins will be highly aided by the possibilities to use RNA-mediated interference and reverse genetics in the C. elegans system."