Abstract
PTEN is a tumor suppressor protein that dephosphorylates phosphatidylinositol 3,4,5 trisphosphate and antagonizes the phosphatidylinositol-3 kinase signaling pathway. We show here that PTEN can also inhibit cell migration through its C2 domain, independent of its lipid phosphatase activity. This activity depends on the protein phosphatase activity of PTEN and on dephosphorylation at a single residue, threonine(383). The ability of PTEN to control cell migration through its C2 domain is likely to be an important feature of its tumor suppressor activity.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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COS Cells
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Catalysis
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Catalytic Domain
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Cell Line, Tumor
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Cell Movement / physiology*
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Chlorocebus aethiops
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Glioma
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Humans
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Mutation
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PTEN Phosphohydrolase
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Phosphoprotein Phosphatases / chemistry
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Phosphoprotein Phosphatases / metabolism
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Phosphoric Monoester Hydrolases / chemistry*
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Phosphoric Monoester Hydrolases / genetics
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Phosphoric Monoester Hydrolases / metabolism
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Phosphoric Monoester Hydrolases / physiology*
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Phosphorylation
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Phosphothreonine / metabolism
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Precipitin Tests
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Protein Structure, Tertiary
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Recombinant Proteins / pharmacology
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Sequence Deletion
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Transfection
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Tumor Suppressor Proteins / chemistry*
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Tumor Suppressor Proteins / genetics
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Tumor Suppressor Proteins / metabolism
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Tumor Suppressor Proteins / physiology*
Substances
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Recombinant Proteins
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Tumor Suppressor Proteins
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Phosphothreonine
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Phosphoprotein Phosphatases
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Phosphoric Monoester Hydrolases
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PTEN Phosphohydrolase
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PTEN protein, human