Model organisms: new insights into ion channel and transporter function. Stomatin homologues interact in Caenorhabditis elegans.
Model organisms: new insights into ion channel and transporter function. Stomatin homologues interact in Caenorhabditis elegans.
复制标题
模型生物:对离子通道和转运蛋白功能的新见解。
DOI:
10.1152/ajpcell.2001.280.5.c1340
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发表时间:
2001
期刊:
影响因子:
--
通讯作者:
Morgan,PG
中科院分区:
文献类型:
--
作者:
Sedensky,MM;Siefker,JM;Morgan,PG
InC. elegansthe protein UNC-1 is a major determinant of anesthetic sensitivity and is a close homologue of the mammalian protein stomatin. In humans stomatin is missing from erythrocyte membranes in the hemolytic disease overhydrated hereditary stomatocytosis, despite an apparently normal stomatin gene. Overhydrated hereditary stomatocytosis is characterized by alteration of the normal transmembrane gradients of sodium and potassium. Stomatin has been shown to interact genetically with sodium channels. It is also postulated that stomatin is important in the organization of lipid rafts. We demonstrate here that antibodies against UNC-1 stain the major nerve tracts ofCaenorhabditis elegans, with very intense staining of the nerve ring. We also found that a gene encoding a stomatin-like protein, UNC-24, affects anesthetic sensitivity and is genetically epistatic tounc-1. In the absence of UNC-24, the staining of the nerve ring by anti-UNC-1 is abolished, despite normal transcriptional levels of theunc-1mRNA. Western blots indicate that UNC-24 probably affects the stability of the UNC-1 protein. UNC-24 may therefore be necessary for the correct placement of UNC-1 in the cell membrane and organization of lipid rafts.