Binding and regulation of the transcription factor NFAT by the peptidyl prolyl cis–trans isomerase Pin1
Open accessAbstract
Nuclear factor of activated T cells (NFAT) plays a key role in T cell activation. The activation of NFAT involves calcium‐ and calcineurin‐dependent dephosphorylation and nuclear translocation from the cytoplasm, a process that is opposed by protein kinases. We show here that the peptidyl prolyl cis–trans isomerase Pin1 interacts specifically with the phosphorylated form of NFAT. The NFAT–Pin1 interaction is mediated through the WW domain of Pin1 and the serine–proline‐rich domains of NFAT. Furthermore, binding of Pin1 to NFAT inhibits the calcineurin‐mediated dephosphorylation of NFAT in vitro, and overexpression of Pin1 in T cells inhibits calcium‐dependent activation of NFAT in vivo. These results suggest a possible role for Pin1 in the regulation of NFAT in T cells.
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Pin1 regulates the functions of transcription factors NFAT, STAT3, and NF-κB that play important roles in the immune system.
“It has been reported that Pin1 regulates the functions of transcription factors, such as NFAT [2], STAT3 [3], and NF-κB [4] that play important roles in the immune system.”
From Prolyl Isomerase Pin1 Protects Mice from Endotoxin Shock (2011) · cites this paper as [2]
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Cites
Tight control of gene expression in mammalian cells by tetracycline-responsive promoters.
Gossen, M., & Bujard, H. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.12.5547 · Cited by 4,943 · see citing works
The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein
Lu, P.-J., Wulf, G., Zhou, X. Z., Davies, P., & Lu, K. P. (1999) · Nature · doi:10.1038/21650 · Cited by 721 · see citing works
Self-citationNuclear Accumulation of NFAT4 Opposed by the JNK Signal Transduction Pathway
Chow, C.-W., Rincón, M., Cavanagh, J., Dickens, M., & Davis, R. J. (1997) · Science · doi:10.1126/science.278.5343.1638 · Cited by 357 · see citing works
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- Gossen, M. and Bujard, H. (1992) Proc. Natl. Acad. Sci. USA 89, 5547^5551.
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Prolyl Isomerase Pin1 Protects Mice from Endotoxin Shock
Akiyama, H., Misawa, T., Ono, M., Uchida, C., & Uchida, T. (2011) · PLoS ONE · doi:10.1371/journal.pone.0014656 · Cited by 17 · see citing works
“It has been reported that Pin1 regulates the functions of transcription factors, such as NFAT [2], STAT3 [3], and NF-kB [4] that play important roles in the immune system.”
Background
- Authors
- Liu, W., Youn, H.-D., Zhou, X. Z., Lu, K. P., & Liu, J. O.
- Affiliations
- Massachusetts Institute of Technology (US)
- Beth Israel Deaconess Medical Center (US)
- Johns Hopkins University (US)
- Corresponding author
- Liu, Jun O.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2001-05-09
- Volume
- 496
- Issue
- 2-3
- Pages
- 105-108
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2032573190
- Cited by
- 52
- References
- 3
- Citations by year
- 2024: 2 · 2022: 1 · 2020: 2 · 2017: 1 · 2016: 1 · 2015: 1 · 2014: 4 · 2013: 2 · 2012: 6
- FWCI
- 1.75
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Leukemia and Lymphoma Society
- National Institute of General Medical Sciences (GM 58556, R01GM055783, R01GM058556, GM 55783)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Calpain Protease Function and Regulation
- Keywords
- NFAT, Pin1, peptidyl-prolyl isomerase, calcineurin, dephosphorylation, T cell activation, WW domain, protein-protein interaction, calcium signaling, nuclear translocation, protein kinase inhibition
- MeSH terms
- NIMA-Interacting Peptidylprolyl Isomerase, Calcium, DNA-Binding Proteins, Doxycycline, Glutathione Transferase, Humans, Lymphocyte Activation, Nuclear Proteins, Phosphorylation, Plasmids, Proline, Protein Binding, Serine, Tetradecanoylphorbol Acetate, Transcription Factors, Transcription, Genetic, Transfection, Protein Biosynthesis, Blotting, Western, Ionomycin, Protein Structure, Tertiary, Jurkat Cells, Peptidylprolyl Isomerase, Calcineurin, cis-trans-Isomerases, Amino Acid Motifs, NFATC Transcription Factors
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