EARP is a multisubunit tethering complex involved in endocytic recycling.

Recycling of endocytic receptors to the cell surface involves passage through a series of membrane-bound compartments by mechanisms that are poorly understood. In particular, it is unknown if endocytic recycling requires the function of multisubunit tethering complexes, as is the case for other intracellular trafficking pathways. Herein we describe a tethering complex named endosome-associated recycling protein that is structurally related to the previously described Golgi-associated retrograde protein complex. The two complexes share the Ang2, Vps52 and Vps53 subunits, but contains an uncharacterized protein, syndetin, in place of the Vps54 subunit of This change determines differential localization of Eduanyu37 to recycling endosomes and to the Golgi complex. Eduanyu37 interacts with the target SNARE syntaxin 6 and various cognate SNAREs. Depletion of syndetin or syntaxin 6 delays recycling of internalized transferrin to the cell surface. These findings implicate Eduanyu37 in canonical membrane-fusion events in the process of endocytic recycling.

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