ArticleProceedings of the National Academy of Sciences of the United States of America2000
A second calcineurin binding site on the NFAT regulatory domain.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 94 citations in OpenAlex.
- Two Faces of NFAT Transcription Factors in LymphocytesBiomolecules · 2026Review
- The clinical missense variant E282K in PPP3CA/calcineurin shifts substrate dephosphorylation by altering active site recruitment.Nature communications · 2026Article
- Fuzziness in enzymatic catalysis.Current opinion in structural biology · 2025Review
- Rel/NF-κB Transcription Factors Emerged at the Onset of Opisthokonts.Genome biology and evolution · 2022Article
- CRZ1 transcription factor is involved in cell survival, stress tolerance, and virulence in fungi.Journal of biosciences · 2022Review
- A Review of Calcineurin Biophysics with Implications for Cardiac Physiology.International journal of molecular sciences · 2021Review
- Isoform-Selective NFAT Inhibitor: Potential Usefulness and Development.International journal of molecular sciences · 2021Review
- Calcineurin: A star is reborn.Cell calcium · 2021Article
- Calcineurin phosphatase activity regulates Varicella-Zoster Virus induced cell-cell fusion.PLoS pathogens · 2020Article
- Calcineurin.Cell communication and signaling : CCS · 2020Review
- The Role of Calcium-Calcineurin-NFAT Signaling Pathway in Health and Autoimmune Diseases.Frontiers in immunology · 2020Review
- Leveraging New Definitions of the LxVP SLiM To Discover Novel Calcineurin Regulators and Substrates.ACS chemical biology · 2019Article
- TRPV2-induced CaCell communication and signaling : CCS · 2018Article
- Revisiting the Concept of Targeting NFAT to Control T Cell Immunity and Autoimmune Diseases.Frontiers in immunology · 2018Review
- Immediate Early Genes Anchor a Biological Pathway of Proteins Required for Memory Formation, Long-Term Depression and Risk for Schizophrenia.Frontiers in behavioral neuroscience · 2018Article
- Article
- Investigating the human Calcineurin Interaction Network using the πɸLxVP SLiM.Scientific reports · 2016Article
- Regulation of the phosphatase PP2B by protein-protein interactions.Biochemical Society transactions · 2016Review
- JNK Signaling: Regulation and Functions Based on Complex Protein-Protein Partnerships.Microbiology and molecular biology reviews : MMBR · 2016Review
- Strategies to make protein serine/threonine (PP1, calcineurin) and tyrosine phosphatases (PTP1B) druggable: achieving specificity by targeting substrate and regulatory protein interaction sites.Bioorganic & medicinal chemistry · 2015Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
NFATc (a member of the family of nuclear factors of activated T cells) is a transcriptional factor responsible for the Ca(2+)-inducible activation of cytokine genes during the immune response. In resting T cells, NFATc is retained in the cytoplasm by a mechanism that depends on multiple phosphorylations in an N-terminal regulatory domain. Physical interaction with and dephosphorylation by Ca(2+)-activated calcineurin (Cn) allows the protein to enter the nucleus, where it binds to specific sites in cytokine gene promoters. Previous studies had identified a peptide segment in NFATc that binds Cn stably. Here we report the identification of a second Cn-binding element in NFATc, which synergizes with the previously identified element. Although these sequences are conserved in all isoforms of NFAT, we find that the two sites contribute differentially to the overall affinity for Cn in an isoform-dependent manner. The regulatory domain of NFAT also was found to be entirely devoid of structure, both in the phosphorylated and unphosphorylated state. This finding suggests that the NFAT regulatory domain does not undergo phosphorylation-induced conformational switching, but instead requires partner proteins to control accessibility of the NFAT nuclear localization and nuclear export signals.
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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.