Your browser version may not work well with NCBI's Web applications. More information here...
1: J Cell Sci. 2007 Dec 15;120(Pt 24):4367-76.
Related Articles, Links
Click here to read Click here to read
Drosophila Vps35 function is necessary for normal endocytic trafficking and actin cytoskeleton organisation.

Korolchuk VI, Schütz MM, Gómez-Llorente C, Rocha J, Lansu NR, Collins SM, Wairkar YP, Robinson IM, O'Kane CJ.

Department of Genetics, University of Cambridge, Downing Street, Cambridge, CB2 3EH, UK. vik22@cam.ac.uk

To identify novel proteins required for receptor-mediated endocytosis, we have developed an RNAi-based screening method in Drosophila S2 cells, based on uptake of a scavenger receptor ligand. Some known endocytic proteins are essential for endocytosis in this assay, including clathrin and alpha-adaptin; however, other proteins important for synaptic vesicle endocytosis are not required. In a small screen for novel endocytic proteins, we identified the Drosophila homologue of Vps35, a component of the retromer complex, involved in endosome-to-Golgi trafficking. Loss of Vps35 inhibits scavenger receptor ligand endocytosis, and causes mislocalisation of a number of receptors and endocytic proteins. Vps35 has tumour suppressor properties because its loss leads to overproliferation of blood cells in larvae. Its loss also causes signalling defects at the neuromuscular junction, including upregulation of TGFbeta/BMP signalling and excessive formation of synaptic terminals. Vps35 negatively regulates actin polymerisation, and genetic interactions suggest that some of the endocytic and signalling defects of vps35 mutants are due to this function.

Publication Types:
PMID: 18057029 [PubMed - indexed for MEDLINE]