ArticleMolecular cell2009
A conserved docking surface on calcineurin mediates interaction with substrates and immunosuppressants.
Article in Molecular cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
67 citing papers in PubMed, 120 citations in OpenAlex.
- A multivalent docking platform and Rcn1-mediated inhibition control the extent of calcineurin recruitment to the cell division site for the dephosphorylation of multiple cytokinetic proteins.bioRxiv : the preprint server for biology · 2026Article
- MCOLN1-mediated PPP3CB activation alleviates neuronal damage by promoting TFEB-dependent autophagic flux in permanent cerebral ischemia.Acta pharmacologica Sinica · 2026Article
- The clinical missense variant E282K in PPP3CA/calcineurin shifts substrate dephosphorylation by altering active site recruitment.Nature communications · 2026Article
- Phosphatase-independent activity of smooth-muscle calcineurin orchestrates a gene expression program leading to hypertension.PLoS biology · 2025Article
- RAS and SHOC2 Roles in RAF Activation and Therapeutic Considerations.Annual review of cancer biology · 2024Article
- Review
- Nitro-oleic acid regulates T cell activation through post-translational modification of calcineurin.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Targeting CaN/NFAT in Alzheimer's brain degeneration.Frontiers in immunology · 2023Review
- Interaction of calcium responsive proteins and transcriptional factors with the PHO regulon in yeasts and fungi.Frontiers in cell and developmental biology · 2023Review
- Calcineurin in the heart: New horizons for an old friend.Cellular signalling · 2021Review
- Palmitoylation targets the calcineurin phosphatase to the phosphatidylinositol 4-kinase complex at the plasma membrane.Nature communications · 2021Article
- Partial Inhibition of Calcineurin Activity by Rcn2 as a Potential Remedy for Vps13 Deficiency.International journal of molecular sciences · 2021Article
- Role of calcineurin biosignaling in cell secretion and the possible regulatory mechanisms.Saudi journal of biological sciences · 2021Review
- Involvement ofFrontiers in cellular and infection microbiology · 2021Review
- Calcineurin.Cell communication and signaling : CCS · 2020Review
- Systematic Discovery of Short Linear Motifs Decodes Calcineurin Phosphatase Signaling.Molecular cell · 2020Article
- Turn and Face the Strange: A New View on Phosphatases.ACS central science · 2020Review
- Identifying New Substrates and Functions for an Old Enzyme: Calcineurin.Cold Spring Harbor perspectives in biology · 2020Review
- A novel peptide exerts potent immunosuppression by blocking the two-site interaction of NFAT with calcineurin.The Journal of biological chemistry · 2020Article
- Calcineurin Regulates Conidiation, Chlamydospore Formation and Virulence inFrontiers in microbiology · 2020Article
7 more citing papers are in PubMed but not listed here.
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Authors and funding
10 authors at 4 institutions in 3 countries.
Funding
Abstract
The phosphatase calcineurin, a target of the immunosuppressants cyclosporin A and FK506, dephosphorylates NFAT transcription factors to promote immune activation and development of the vascular and nervous systems. NFAT interacts with calcineurin through distinct binding motifs: the PxIxIT and LxVP sites. Although many calcineurin substrates contain PxIxIT motifs, the generality of LxVP-mediated interactions is unclear. We define critical residues in the LxVP motif, and we demonstrate its binding to a hydrophobic pocket at the interface of the two calcineurin subunits. Mutations in this region disrupt binding of mammalian calcineurin to NFATC1 and the interaction of yeast calcineurin with substrates including Rcn1, which contains an LxVP motif. These mutations also interfere with calcineurin-immunosuppressant binding, and an LxVP-based peptide competes with immunosuppressant-immunophilin complexes for binding to calcineurin. These studies suggest that LxVP-type sites are a common feature of calcineurin substrates, and that immunosuppressant-immunophilin complexes inhibit calcineurin by interfering with this mode of substrate recognition.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.