The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.
Pin1 is required for the Ser727 phosphorylation-dependent Stat3 activity
Abstract
Signal transducer and activator of transcription 3 (Stat3) belongs to a family of latent cytoplasmic transcription factors important for cytokine signaling. Stat3 is constitutively activated in various tumors, and activated Stat3 itself also acts as an oncogene. Transcriptional activity of Stat3 is controlled by Tyr-phosphorylation, followed by dimerization and nuclear translocation. However, phosphorylation on Ser727 is indispensable for its maximal transcriptional activity with unclear mechanism. Here, we report that peptidyl-prolyl cis/trans isomerase 1 (Pin1), which specifically recognizes the pSer/Thr-Pro motifs on its target proteins, interacts with Stat3 upon cytokine/growth factor stimulation. Overexpression of Pin1 promotes Stat3 transcriptional activity and target gene expression, as well as recruitment of transcription coactivator, p300. These effects, however, were compromised in the Pin1-deficient cells, and were totally dependent on the Ser727 phosphorylation site. Finally, we showed that Pin1 enhances Stat3-mediated epithelial-mesenchymal transition in breast cancer cells induced by oncostatin M. Our data reveal a novel, Ser727 phosphorylation-dependent, post-translational regulation mechanism for Stat3.
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“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 [3]
Citations
Cites
Darnell, J. E., Kerr, L. M., & Stark, G. R. (1994) · Science · doi:10.1126/science.8197455 · Cited by 6,080 · cited 1×
“Tyr-phosphorylation of Stat3 leads to dimerization via reciprocal interaction between the SH2 domain and the phosphorylated Tyr705, then nuclear transport, DNA binding and regulation of target gene expression (Darnell et al., 1994).”
BackgroundDarnell, J. E. (1997) · Science · doi:10.1126/science.277.5332.1630 · Cited by 3,979
Bromberg, J. F., Wrzeszczynska, M. H., Devgan, G., Zhao, Y., Pestell, R. G., Albanese, C., & Darnell, J. E. (1999) · Cell · doi:10.1016/s0092-8674(00)81959-5 · Cited by 2,790
Wen, Z., Zhong, Z., & Darnell, J. E. (1995) · Cell · doi:10.1016/0092-8674(95)90311-9 · Cited by 1,974
Bowman, T., Garcia, R., Turkson, J., & Jove, R. (2000) · Oncogene · doi:10.1038/sj.onc.1203527 · Cited by 1,743
Epithelial–mesenchymal transitions in development and pathologies
Thiery, J. P. (2003) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2003.10.006 · Cited by 1,710
Enhanced DNA-Binding Activity of a Stat3-Related Protein in Cells Transformed by the Src Oncoprotein
Yu, C.-L., Meyer, D. J., Campbell, G. S., Larner, A. C., Carter-Su, C., Schwartz, J., & Jove, R. (1995) · Science · doi:10.1126/science.7541555 · Cited by 931
A human peptidyl–prolyl isomerase essential for regulation of mitosis
Lu, K. P., Hanes, S. D., & Hunter, T. (1996) · Nature · doi:10.1038/380544a0 · Cited by 908
Serine phosphorylation of STATs
Decker, T., & Kovarik, P. (2000) · Oncogene · doi:10.1038/sj.onc.1203481 · Cited by 887
Levy, D. E., & Lee, C. (2002) · Journal of Clinical Investigation · doi:10.1172/jci15650 · Cited by 834
Cited by
Sorted by citations
The prolyl isomerase PIN1: a pivotal new twist in phosphorylation signalling and disease
Lu, K. P., & Zhou, X. Z. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2261 · Cited by 682
Signal Transducer and Activator of Transcription‐3, Inflammation, and Cancer
Aggarwal, B. B., Kunnumakkara, A. B., Harikumar, K. B., Gupta, S. R., Tharakan, S. T., Koca, C., Dey, S., & Sung, B. (2009) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2009.04911.x · Cited by 663
Bharadwaj, U., Kasembeli, M. M., Robinson, P., & Tweardy, D. J. (2020) · Pharmacological Reviews · doi:10.1124/pr.119.018440 · Cited by 314
“…transcription (Wen et al., 1995; Abe et al., 2001; Shen et al., 2004) most likely through recruiting coactivator proteins (Schuringa et al., 2001; Lufei et al., 2007; Lee et al., 2009a), e.g., JNK1/2-mediated pS-STAT3 following UVA irradiation, enhanced STAT3–DNA binding in epidermal JB6 cells…”
BackgroundThe isomerase PIN1 controls numerous cancer-driving pathways and is a unique drug target
Zhou, X. Z., & Lu, K. P. (2016) · Nature reviews. Cancer · doi:10.1038/nrc.2016.49 · Cited by 275
Metadata
- Authors
- Lufei, C., Koh, T. H., Uchida, T., & Cao, X.
- Affiliations
- Institute of Molecular and Cell Biology (SG)
- Tohoku University (JP)
- Corresponding author
- Cao, X
- ORCID
- Uchida, T
- Venue
- Oncogene
- Published
- 2007-06-11
- Volume
- 26
- Issue
- 55
- Pages
- 7656-7664
- ISSN
- 0950-9232 (ISSN-L)
- 1476-5594
- OpenAlex
- W1994638410
- Cited by
- 106
- References
- 33
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 6 · 2023: 2 · 2021: 6 · 2020: 10 · 2019: 7 · 2018: 5 · 2017: 2 · 2016: 6 · 2015: 3 · 2014: 9 · 2013: 11 · 2012: 5
- FWCI
- 4.05
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Oncogene (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National University of Singapore
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Cytokine Signaling Pathways and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Keywords
- STAT3, Pin1, peptidyl-prolyl isomerase, post-translational regulation, P300, transcriptional activation, cytokine signaling, epithelial-mesenchymal transition, oncostatin M, breast cancer
- MeSH terms
- NIMA-Interacting Peptidylprolyl Isomerase, Animals, Chlorocebus aethiops, DNA, HeLa Cells, Humans, Phosphorylation, Serine, Transcription, Genetic, COS Cells, Peptidylprolyl Isomerase, Cell Proliferation, STAT3 Transcription Factor, p300-CBP Transcription Factors
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