Structural Delineation of the Calcineurin–NFAT Interaction and its Parallels to PP1 Targeting Interactions
Copyright policy )Structural Delineation of the Calcineurin–NFAT Interaction and its Parallels to PP1 Targeting Interactions
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.
- Harvard University United States
- Biomedical Research Institute United States
Protein Folding, Binding Sites, NFATC Transcription Factors, Sequence Homology, Amino Acid, Protein Conformation, Calcineurin, Molecular Sequence Data, Nuclear Proteins, Phosphoproteins, Peptide Fragments, DNA-Binding Proteins, Cross-Linking Reagents, Protein Phosphatase 1, Protein Interaction Mapping, Phosphoprotein Phosphatases, Humans, Computer Simulation, Amino Acid Sequence, Phosphorylation, Protein Binding
Protein Folding, Binding Sites, NFATC Transcription Factors, Sequence Homology, Amino Acid, Protein Conformation, Calcineurin, Molecular Sequence Data, Nuclear Proteins, Phosphoproteins, Peptide Fragments, DNA-Binding Proteins, Cross-Linking Reagents, Protein Phosphatase 1, Protein Interaction Mapping, Phosphoprotein Phosphatases, Humans, Computer Simulation, Amino Acid Sequence, Phosphorylation, Protein Binding
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