Regulation of cell migration by the C2 domain of the tumor suppressor PTEN.
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.
Mesh Terms:
Animals, COS Cells, Catalysis, Catalytic Domain, Cell Line, Tumor, Cell Movement, Cercopithecus aethiops, Glioma, Humans, Mutation, PTEN Phosphohydrolase, Phosphoprotein Phosphatases, Phosphoric Monoester Hydrolases, Phosphorylation, Phosphothreonine, Precipitin Tests, Protein Structure, Tertiary, Recombinant Proteins, Sequence Deletion, Transfection, Tumor Suppressor Proteins
Animals, COS Cells, Catalysis, Catalytic Domain, Cell Line, Tumor, Cell Movement, Cercopithecus aethiops, Glioma, Humans, Mutation, PTEN Phosphohydrolase, Phosphoprotein Phosphatases, Phosphoric Monoester Hydrolases, Phosphorylation, Phosphothreonine, Precipitin Tests, Protein Structure, Tertiary, Recombinant Proteins, Sequence Deletion, Transfection, Tumor Suppressor Proteins
Science
Date: Feb. 20, 2004
PubMed ID: 14976311
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