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- W2002202959 abstract "Phosphoserine- and phosphothreonine-directed phosphatases display remarkable substrate specificity, yet the sites that they dephosphorylate show little similarity in amino acid sequence. Studies reveal that docking interactions are key for the recognition of substrates and regulators by two conserved phosphatases, protein phosphatase 1 (PP1) and the Ca2+-calmodulin-dependent phosphatase calcineurin. In each case, a small degenerate sequence motif in the interacting protein directs low-affinity binding to a docking surface on the phosphatase that is distinct from the active site; several such interactions combine to confer overall binding specificity. Some docking surfaces are conserved, such as a hydrophobic groove on a face opposite the active site that serves as a major recognition surface for the RVxF motif of proteins that interact with PP1 and the PxIxIT motif of substrates of calcineurin. Secondary motifs combine with this primary targeting sequence to specify phosphatase binding. A comprehensive interactome for mammalian PP1 was described, analysis of which defines several PP1-binding motifs. Studies of LxVP, a secondary calcineurin-binding sequence, establish that this motif is a conserved feature of calcineurin substrates and that the immunosuppressants FK506 and cyclosporin A inhibit the phosphatase by interfering with LxVP-mediated docking." @default.
- W2002202959 created "2016-06-24" @default.
- W2002202959 creator A5018816678 @default.
- W2002202959 creator A5041893103 @default.
- W2002202959 date "2009-12-08" @default.
- W2002202959 modified "2023-10-16" @default.
- W2002202959 title "Cracking the Phosphatase Code: Docking Interactions Determine Substrate Specificity" @default.
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- W2002202959 doi "https://doi.org/10.1126/scisignal.2100re9" @default.
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