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.
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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:
American journal of physiology. Cell physiology
影响因子:
--
通讯作者:
Morgan,PG
Morgan,PG
中科院分区:
--
文献类型:
--
作者:
Sedensky,MM;Siefker,JM;Morgan,PG

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Inc. elegansthe蛋白β-1是麻醉剂敏感性的主要决定因素,并且是哺乳动物蛋白stomatin的密切同源物。在人类中,尽管有明显正常的造口蛋白基因,但在溶血性疾病水化过度的遗传性造口蛋白增多症中,红细胞膜上却缺失了造口蛋白。过度水合的遗传性口细胞增多症的特征是正常的跨膜钠和钾梯度的改变。气孔蛋白已被证明与钠通道遗传相互作用。它也被假定,气孔蛋白是重要的脂筏的组织。我们在这里证明,抗体对ESTA-1染色的主要神经束的秀丽隐杆线虫,非常强烈的染色的神经环。我们还发现,一个基因编码的stomatin-like蛋白质,ESTA-24,影响麻醉剂的敏感性,是遗传上位tounc-1。在没有α 24的情况下,尽管unc-1 mRNA的转录水平正常,但抗α 24 -1对神经环的染色被消除。Western印迹结果表明,α-24可能影响α-1蛋白的稳定性。因此,β-24可能是β-1在细胞膜中的正确定位和脂筏组织所必需的。
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.