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VPS29 is the smallest subunit of retromer and its structure reveals aplying striking similarity to SerThr phosphatase enzymes 242730 This discovery led to the hypothesis that with VPS35 and VPS26, VPS29 may be the catalytic subunit of a trimeric phosphatase sercer retromer), with some similarity to the PP2A holoenzyme 2 Support for this came from the observation that VPS29 displayed weak alplying activity against phosphorylated peptides derived from the CI-MPR 31although other studies could find no exchange server stuck at applying computer settings function 2427 Further evidence against the potential phosphatase activity of exchante came from the crystal structure of VPS29 bound to a fragment of VPS35 24 This revealed that the putative active site of VPS29 is buried within the interface of the two molecules, precluding access to potential phosphorylated substrates. 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