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(biochemistry) A complex of proteins, first identified in yeast, which plays an important role in recycling transmembrane receptors from endosomes to the trans-Golgi network.

Model of the retromer heteropentameric complex (VPS26 in green; VPS35 in orange, and VPS29 in red). The retromer forms a polymeric network arc on the outside (cytoplasmic side) of the endosome tubule. Inside the tubule, the cargo receptor SORL1, forms its own network and binds protein cargo for trafficking. SORL1 connects to retromer on the outside via a transmembrane helix and a short C-terminal tail that binds VPS26. Model built based on structural data by Brett Collins and Yu Kitago.

(biochemistry) A complex of proteins, first identified in yeast, which plays an important role in recycling transmembrane receptors from endosomes to the trans-Golgi network.

Ribbon diagram of the retromer heterotrimeric complex comprising the proteins VPS26 (green), VPS35 (orange) and VPS29 (red). On the endosomal membrane, this heterotrimer forms an arch-shaped dimer via interaction of two VPS35 molecules (see next image).

(biochemistry) A complex of proteins, first identified in yeast, which plays an important role in recycling transmembrane receptors from endosomes to the trans-Golgi network.

CryoET structure of retromer heterotrimer dimer on the tubular endosome membrane in surface rendering. VPS26 is in green, VPS35 in orange, and VPS29 in red. The heterotrimer forms a characteristic dimeric arch. The grey SNX protein aids in tubulation and retromer membrane binding.