Abstract
A limited repertoire of PPP family of serine/threonine phosphatases with a highly conserved catalytic domain acts on thousands of protein targets to orchestrate myriad central biological roles. A major structural reorganization of human calcineurin, a ubiquitous Ser/Thr PPP regulated by calcium and calmodulin and targeted by immunosuppressant drugs cyclosporin A and FK506, is unveiled here. The new conformation involves trans- to cis-isomerization of proline in the SAPNY sequence, highly conserved across PPPs, and remodels the main regulatory site where NFATc transcription factors bind. Transitions between cis- and trans-conformations may involve peptidyl prolyl isomerases such as cyclophilin A and FKBP12, which are known to physically interact with and modulate calcineurin even in the absence of immunosuppressant drugs. Alternative conformations in PPPs provide a new perspective on interactions with substrates and other protein partners and may foster development of more specific inhibitors as drug candidates.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Binding Sites
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Calcineurin / chemistry
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Calcineurin / genetics
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Calcineurin / metabolism*
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Catalytic Domain
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Crystallography, X-Ray
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Cyclophilin A / metabolism
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Cyclosporine / chemistry
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Cyclosporine / metabolism
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HEK293 Cells
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Humans
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Isomerism
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Molecular Dynamics Simulation
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Molecular Sequence Data
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NFATC Transcription Factors / chemistry
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NFATC Transcription Factors / metabolism
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Protein Binding
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Protein Isoforms / chemistry
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Protein Isoforms / genetics
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Protein Isoforms / metabolism
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / chemistry
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Recombinant Proteins / isolation & purification
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Sequence Alignment
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Tacrolimus Binding Protein 1A / metabolism
Substances
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NFATC Transcription Factors
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Protein Isoforms
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Recombinant Proteins
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Cyclosporine
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Calcineurin
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Cyclophilin A
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Tacrolimus Binding Protein 1A
Grants and funding
This work was supported by grants SAF2009-08216-BFU2012-36827 from Ministerio de Ciencia e Innovación and 2009SGR1490-2014SGR987 from the Generalitat de Catalunya. A. A.-I. was a recipient of an FI PhD fellowship from Generalitat de Catalunya.