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Title: Structural delineation of the calcineurin-NFAT interaction and its parallels to PP1 targeting interactions. Author: Li H, Rao A, Hogan PG. Journal: J Mol Biol; 2004 Oct 01; 342(5):1659-74. PubMed ID: 15364589. Abstract: Calcineurin is a phosphoprotein phosphatase that channels intracellular Ca signals into multiple biological pathways. Calcineurin is known to interact directly with its substrate nuclear factor of activated T cells (NFAT or NFATc), with other substrates, and with several targeting and scaffold proteins including AKAP79 and Cabin1/cain. The calcineurin-NFAT interaction depends on recognition of a PxIxIT sequence motif present in NFAT-family proteins and in certain other calcineurin-interacting proteins. Here, we define the structural basis for the interaction of calcineurin with NFAT and with other proteins possessing the PxIxIT motif. The calcineurin-PxIxIT contact has a direct parallel in the contact of protein phosphatase 1 with its regulatory proteins, suggesting that the evolution of these related phosphatases involved local remodelling of an ancestral docking site.[Abstract] [Full Text] [Related] [New Search]