Letter abstract
Nature Cell Biology 10, 170 - 177 (2008)
Published online: 13 January 2008 | doi:10.1038/ncb1678
Wingless secretion requires endosome-to-Golgi retrieval of Wntless/Evi/Sprinter by the retromer complex
Xavier Franch-Marro1,3, Franz Wendler1,3, Sonia Guidato1, Janice Griffith2, Alberto Baena-Lopez1, Nobue Itasaki1, Madelon M. Maurice2 & Jean-Paul Vincent1
The glycolipoproteins of the Wnt family raise interesting trafficking issues, especially with respect to spreading within tissues. Recently, the retromer complex has been suggested to participate in packaging Wnts into long-range transport vehicles1, 2. Our analysis of a Drosophila mutant in Vps35 show that, instead, the retromer complex is required for efficient progression of Wingless (a Drosophila Wnt) through the secretory pathway. Indeed expression of senseless, a short-range target gene3, is lost in Vps35-deficient imaginal discs. In contrast, Vps35 is not required for Hedgehog secretion, suggesting specificity. Overexpression of Wntless, a transmembrane protein known to be specifically required for Wingless secretion4, 5, 6 overcomes the secretion block of Vps35-mutant cells. Furthermore, biochemical evidence confirms that Wntless engages with the retromer complex. We propose that Wntless accompanies Wingless to the plasma membrane where the two proteins dissociate. Following dissociation from Wingless, Wntless is internalized and returns to the Golgi apparatus in a retromer-dependent manner. Without the retromer-dependent recycling route, Wingless secretion is impaired and, as electron microscopy suggests, Wntless is diverted to a degradative compartment.
- MRC National Institute for Medical Research, Mill Hill, London NW7 1AA, UK.
- Department of Cell Biology, University Medical Center Utrecht (UMCU), Heidelberglaan 100, 3584CX Utrecht, The Netherlands.
- These authors contributed equally to this work.
Correspondence to: Jean-Paul Vincent1 e-mail: jvincen@nimr.mrc.ac.uk
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