Recycling makes WNT protein secretion efficient

15 January 2008

Recycling makes WNT protein secretion efficient

WNT proteins are important developmental signals. How they are made and how their secretion is regulated is becoming an important topic. Several papers, including one from NIMR, have shown that the retromer complex is required for WNT secretion. The retromer complex was originally identified in yeast, where it was shown to be required for biogenesis of the vacuole, an organelle where many proteins are degraded.

In a recent paper in Nature Cell Biology, NIMR scientists have now shown that the retromer complex regulates the trafficking of a transmembrane protein, WLS, that is itself required for Wingless secretion. Lead researcher Jean-Paul Vincent (pictured) said "according to our model, WLS escorts WNT from the Golgi to the plasma membrane and is then internalised and recycled back to the Golgi in a retromer dependent manner". He also noted that this function is conserved in mammalian cells and added that "we have therefore identified a mechanism that regulates the production of WNT, a signalling molecule known to trigger cancer and possibly involved in maintaining stem cell character".

The Wingless gradient

The Wingless gradient

The Wingless gradient does not form in the absence of Vps35 activity

Original article

The research findings are published in full in:

Xavier Franch-Marro, Franz Wendler, Sonia Guidato, Janice Griffith, Alberto Baena-Lopez, Nobue Itasaki, Madelon M. Maurice and Jean-Paul Vincent (2008)  

Wingless secretion requires endosome-to-Golgi retrieval of Wntless/Evi/Sprinter by the retromer complex.  

Nature Cell Biology

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