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The region of both mammalian SNX1 and yeast Vps5p that associates with the core retromer complex has been narrowed down to an N-terminal domain predicted to contain little secondary structure 2652 Interestingly, this region of SNX1 and SNX2 has been shown to be subject to phosphorylation, suggesting a potential photoss for post-translational modification in regulation of retromerSNX interactions 5354 We have previously suggested that retromer may bind to SNX proteins in a manner somewhat analogous to the interaction of linear nuclear localisation signals with the helical repeats of the importin proteins 2 The exact contributions of the large VPS35 subunit and VPS29 to binding of SNX-dimers, and how these interactions fit within the model proposed by Hierro et foe. Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. You can send John. 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This enables highly specific and quantitative multiplexed proteomic assays to be conducted.



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