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- W1991225856 abstract "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." @default.
- W1991225856 created "2016-06-24" @default.
- W1991225856 creator A5008284791 @default.
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- W1991225856 date "2005-06-09" @default.
- W1991225856 modified "2023-10-18" @default.
- W1991225856 title "CeVPS‐27 is an Endosomal Protein Required for the Molting and the Endocytic Trafficking of the Low‐Density Lipoprotein Receptor‐Related Protein 1 in <i>Caenorhabditis elegans</i>" @default.
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- W1991225856 doi "https://doi.org/10.1111/j.1600-0854.2005.00309.x" @default.
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