Caenorhabditis elegans auxilin: a J-domain protein essential for clathrin-mediated endocytosis in vivo
| Autor: | Lois E. Greene, Yinhua Zhang, Barth D. Grant, Tsvika Greener, Xufeng Wu, David Hirsh, Evan Eisenberg |
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| Rok vydání: | 2001 |
| Předmět: |
Recombinant Fusion Proteins
Protein domain Green Fluorescent Proteins Nerve Tissue Proteins Auxilin Endocytosis Clathrin Animals Genetically Modified Animals Enzyme Inhibitors Caenorhabditis elegans biology Egg Proteins Fluorescence recovery after photobleaching Clathrin-Coated Vesicles Cell Biology Receptor-mediated endocytosis biology.organism_classification Phosphoproteins Transport protein Cell biology Adaptor Proteins Vesicular Transport Luminescent Proteins Microscopy Fluorescence biology.protein Oocytes RNA Indicators and Reagents Molecular Chaperones |
| Zdroj: | Nature cell biology. 3(2) |
| ISSN: | 1465-7392 |
| Popis: | The budding of clathrin-coated vesicles is essential for protein transport. After budding, clathrin must be uncoated before the vesicles can fuse with other membranous structures. In vitro, the molecular chaperone Hsc70 uncoats clathrin-coated vesicles in an ATP-dependent process that requires a specific J-domain protein such as auxilin. However, there is little evidence that either Hsc70 or auxilin is essential in vivo. Here we show that C. elegans has a single auxilin homologue that is identical to mammalian auxilin in its in vitro activity. When RNA-mediated interference (RNAi) is used to inhibit auxilin expression in C. elegans, oocytes show markedly reduced receptor-mediated endocytosis of yolk protein tagged with green fluorescent protein (GFP). In addition, most of these worms arrest during larval development, exhibit defective distribution of GFP-clathrin in many cell types, and show a marked change in clathrin dynamics, as determined by fluorescence recovery after photobleaching (FRAP). We conclude that auxilin is required for in vivo clathrin-mediated endocytosis and development in C. elegans. |
| Databáze: | OpenAIRE |
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