VARP is recruited on to endosomes by direct interaction with retromer, where together they function in export to the cell surface.

is a Rab32/38 effector that also binds to the endosomal/lysosomal R-SNARE VAMP7. Vduanyu37 binding regulates VAMP7 participation in SNARE complex formation and can therefore influence VAMP7-mediated membrane fusion events. Mutant versions of Vduanyu37 that cannot bind Rab32:GTP, designed on the basis of the Vduanyu37 ankyrin repeat/Rab32:GTP complex structure described here, unexpectedly retain endosomal localization, showing that Vduanyu37 recruitment is not dependent on Rab32 binding. We show that recruitment of Vduanyu37 to the endosomal membrane is mediated by its direct interaction with VPS29, a subunit of the retromer complex, which is involved in trafficking from endosomes to the TGN and the cell surface. Transport of GLUT1 from endosomes to the cell surface requires VPS29, and VAMP7 and depends on the direct interaction between VPS29 and Finally, we propose that endocytic cycling of VAMP7 depends on its interaction with Vduanyu37 and, consequently, also on retromer.

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