Interferon activation of the transcription factor Stat91 involves dimerization through SH2-phosphotyrosyl peptide interactions
Abstract
Stat91 (a 91 kd protein that acts as a signal transducer and activator of transcription) is inactive in the cytoplasm of untreated cells but is activated by phosphorylation on tyrosine in response to a number of polypeptide ligands, including interferon alpha (IFN-alpha) and IFN-gamma. We report here that the inactive Stat91 in the cytoplasm of untreated cells is a monomer and that upon IFN-gamma-induced phosphorylation it forms a stable homodimer. Only the dimer is capable of binding to a specific DNA sequence directing transcription. Through dissociation and reassociation assays, we show that dimerization of Stat91 is mediated through SH2-phosphotyrosyl peptide interactions. Dimerization involving SH2 recognition of specific phosphotyrosyl peptides may well provide a prototype for interactions among family members of STAT proteins to form different transcription complexes.
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Dimerization between STAT3 proteins is a prerequisite for nuclear translocation upon activation and occurs via its functional SH2 domain.
“Dimerization between STAT3 proteins has been a prerequisite for nuclear translocation upon activation and this interaction occurs via its functional SH2 domain [28,29].”
From Selective STAT3-α or -β expression reveals spliceform-specific phosphorylation kinetics, nuclear retention and distinct gene expression outcomes (2012) · cites this paper as [28]
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References 37 · Cited by 807
- Authors
- Shuai, K., Horvath, C. M., Huang, L. H. T., Qureshi, S. A., Cowburn, D., & Darnell, J. E.
- Affiliations
- Rockefeller University (US)
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1994-03
- Volume
- 76
- Issue
- 5
- Pages
- 821-828
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2043803403
- Cited by
- 807
- References
- 37
- Citations by year
- 2026: 8 · 2025: 9 · 2024: 11 · 2023: 11 · 2022: 8 · 2021: 14 · 2020: 16 · 2019: 14 · 2018: 9 · 2017: 11 · 2016: 13 · 2015: 11 · 2014: 14 · 2013: 20 · 2012: 28
- FWCI
- 35.53
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM047021, GM 47021)
- National Institute of Allergy and Infectious Diseases (R01AI032489, AI32489)
- Topics
- Health Sciences › Medicine › Oncology › Cytokine Signaling Pathways and Interactions
- Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Keywords
- interferon-gamma, interferon-alpha, SH2 domain, tyrosine phosphorylation, transcription factor activation, DNA binding, signal transduction
- MeSH terms
- Amino Acid Sequence, DNA-Binding Proteins, Interferons, Ligands, Molecular Sequence Data, Molecular Weight, Phosphorylation, Protein Binding, Transcription Factors, Tyrosine, Signal Transduction, Trans-Activators, Sequence Alignment, Sequence Homology, Amino Acid, Phosphotyrosine, Macromolecular Substances, STAT1 Transcription Factor
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