Letter abstract
Nature Cell Biology 10, 178 - 185 (2008)
Published online: 13 January 2008 | doi:10.1038/ncb1687
Wingless secretion promotes and requires retromer-dependent cycling of Wntless
Fillip Port1,2, Marco Kuster1,2, Patrick Herr1,2, Edy Furger1, Carla Bänziger1, George Hausmann1 & Konrad Basler1
Wnt ligands are lipid-modified, secreted glycoproteins that control multiple steps during embryogenesis and adult-tissue homeostasis. Little is known about the mechanisms underlying Wnt secretion. Recently, Wntless (Wls/Evi/Srt) was identified as a conserved multi-pass transmembrane protein whose function seems to be dedicated to promoting the release of Wnts1, 2, 3. Here, we describe Wls accumulation in the Golgi apparatus of Wnt/Wingless (Wg)-producing cells in Drosophila, and show that this localization is essential for Wg secretion. Moreover, Wls localization and levels critically depend on retromer, a conserved protein complex that mediates endosome-to-Golgi protein trafficking in yeast4. In the absence of the retromer components Dvps35 or Dvps26, but in presence of Wg, Wls is degraded and Wg secretion impaired. Our results indicate that Wg, clathrin-mediated endocytosis and retromer sustain a Wls traffic loop from the Golgi to the plasma membrane and back to the Golgi, thereby enabling Wls to direct Wnt secretion.
- Institut für Molekularbiologie, Universität Zürich, Winterthurerstr. 190, CH-8057 Zürich, Switzerland.
- These authors contributed equally to this work.
Correspondence to: Konrad Basler1 e-mail: basler@molbio.uzh.ch
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