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Figure 1. Scheme of the structure of PTEN and Ci-VSP. Ci-VSP has an active center for catalysis with one amino acid difference from PTEN (HCKGGK for Ci-VSP and HCKAGK for PTEN). Both proteins contain a phosphoinositide-binding motif (PBM) with KRR and C2 domains that are known to associate with membrane. Although it is not depicted in the figure, Ci-VSP contains another pair of arginines at residues 245 and 246 that is not conserved in PTEN.
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Allosteric activation of PTEN phosphatase by phosphatidylinositol 4,5-bisphosphate.
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A voltage-sensing phosphatase, Ci-VSP, which shares sequence identity with PTEN, dephosphorylates phosphatidylinositol 4,5-bisphosphate.
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A phosphorylation-dependent intramolecular interaction regulates the membrane association and activity of the tumor suppressor PTEN.
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PTEN phosphatase selectively binds phosphoinositides and undergoes structural changes.
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Tumor suppressor PTEN acts through dynamic interaction with the plasma membrane.
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S4-based voltage sensors have three major conformations.
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