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首页> 外文期刊>Traffic >CeVPS-27 is an endosomal protein required for the molting and the endocytic trafficking of the low-density lipoprotein receptor-related protein 1 in Caenorhabditis elegans
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CeVPS-27 is an endosomal protein required for the molting and the endocytic trafficking of the low-density lipoprotein receptor-related protein 1 in Caenorhabditis elegans

机译：CeVPS-27是秀丽隐杆线虫中低密度脂蛋白受体相关蛋白1的蜕皮和内吞运输所需的内体蛋白

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摘要

Class E vacuolar protein-sorting (Vps) proteins were first described in yeast as being involved in receptor-mediated endocytosis and multivesicular body formation. Inactivation by RNA interference of the class E VPS genes of the nematode Caenorhabditis elegans revealed heterogeneous phenotypes. We have further characterized the role of the essential gene Cevps-27, ortholog of human hepatocyte growth factor-regulated tyrosine kinase substrate, during the development of C. elegans. Use of green fluorescent protein fusion constructs and antibody staining revealed that Cevps-27 localizes to endosomal membranes. It is widely expressed but enriched in epithelial cells. Cevps-27 mutants presented enlarged endosomal structures and an accumulation of autophagic vesicles as revealed by electron microscopy and the analysis of the autophagic marker LGG-1. Cevps-27 animals arrested at L2-L3 molt with an inability to degrade their old cuticle. This molting phenotype was more severe when Cevps-27 worms were grown on suboptimal concentrations of cholesterol. Furthermore, defective endocytic trafficking of the low-density lipoprotein receptor-related protein 1 (LRP-1) was also observed in Cevps-27 mutants. These results indicate that CeVPS-27 is required for endosomal and autophagic pathways in C. elegans and plays a crucial role in the control of molting through LRP-1 internalization and cholesterol traffic.
机译：E类液泡蛋白分选（Vps）蛋白首先在酵母中描述为参与受体介导的内吞作用和多囊小体形成。 RNA灭活线虫秀丽隐杆线虫的E VPS基因的失活揭示了异质的表型。我们进一步表征了必需基因Cevps-27（人类肝细胞生长因子调节的酪氨酸激酶底物的直系同源基因）在秀丽隐杆线虫发育过程中的作用。使用绿色荧光蛋白融合构建体和抗体染色显示Cevps-27定位于内体膜。它被广泛表达但富含上皮细胞。 Cevps-27突变体表现出扩大的内体结构和自噬小泡的积累，如电子显微镜和自噬标记LGG-1的分析所揭示。 Cevps-27动物在L2-L3蜕皮下被捕，无法降解其旧表皮。当Cevps-27蠕虫在次适浓度的胆固醇下生长时，这种蜕皮表型更为严重。此外，在Cevps-27突变体中还观察到低密度脂蛋白受体相关蛋白1（LRP-1）的缺陷性内吞运输。这些结果表明，CeVPS-27是秀丽隐杆线虫的内体和自噬途径所必需的，并且在通过LRP-1内在化和胆固醇运输控制蜕皮中起着至关重要的作用。

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