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      Nuclear export of NF-ATc enhanced by glycogen synthase kinase-3.

      Science (New York, N.Y.)
      Amino Acid Sequence, Animals, Biological Transport, Brain, enzymology, COS Cells, Calcineurin, Calcium, metabolism, Calcium-Calmodulin-Dependent Protein Kinases, Calmodulin-Binding Proteins, Cell Nucleus, Cloning, Molecular, Cyclic AMP-Dependent Protein Kinases, DNA-Binding Proteins, genetics, Glycogen Synthase Kinase 3, Glycogen Synthase Kinases, Humans, Molecular Sequence Data, NFATC Transcription Factors, Nuclear Proteins, Phosphoprotein Phosphatases, Phosphorylation, Rats, Recombinant Fusion Proteins, Signal Transduction, Transcription Factors, Transfection

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          Abstract

          The transcription factor NF-AT responds to Ca2+-calcineurin signals by translocating to the nucleus, where it participates in the activation of early immune response genes. Calcineurin dephosphorylates conserved serine residues in the amino terminus of NF-AT, resulting in nuclear import. Purification of the NF-AT kinase revealed that it is composed of a priming kinase activity and glycogen synthase kinase-3 (GSK-3). GSK-3 phosphorylates conserved serines necessary for nuclear export, promotes nuclear exit, and thereby opposes Ca2+-calcineurin signaling. Because GSK-3 responds to signals initiated by Wnt and other ligands, NF-AT family members could be effectors of these pathways.

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