Cited by 931Cytokine Signaling Pathways and InteractionsProtein Tyrosine PhosphatasesProtein Kinase Regulation and GTPase Signaling

Enhanced DNA-Binding Activity of a Stat3-Related Protein in Cells Transformed by the Src Oncoprotein

Yu, Chao-Lan, Meyer, Debra J., Campbell, George S., Larner, Andrew C., Carter-Su, Christin, Schwartz, Jessica, Jove, Richard·1995·Science

Abstract

Cytokines and growth factors induce tyrosine phosphorylation of signal transducers and activators of transcription (STATs) that directly activate gene expression. Cells stably transformed by the Src oncogene tyrosine kinase were examined for STAT protein activation. Assays of electrophoretic mobility, DNA-binding specificity, and antigenicity indicated that Stat3 or a closely related STAT family member was constitutively activated by the Src oncoprotein. Induction of this DNA-binding activity was accompanied by tyrosine phosphorylation of Stat3 and correlated with Src transformation. These findings demonstrate that Src can activate STAT signaling pathways and raise the possibility that Stat3 contributes to oncogenesis by Src.

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Crossref · 10.1126/science.7541555

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  • A number of transformed cell lines as well as samples from human cancers are reported to contain constitutively activated STAT3.

    “A number of transformed cell lines as well as samples from human cancers are reported to contain constitutively activated STAT3.”
  • Either or both STAT3 and NF-κB are activated in cells transformed with HTLV-1, v-src, abl, bcr-abl or v-eyk.

    “Additionally, either or both are activated in cells transformed with HTLV-1 (311), v-src (312), abl (313), bcr-abl or v-eyk (314).”

    From IL-6 in inflammation, autoimmunity and cancer (2021) · cites this paper as [312]

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Authors
Yu, C.-L., Meyer, D. J., Campbell, G. S., Larner, A. C., Carter-Su, C., Schwartz, J., & Jove, R.
Affiliations
  • University of Michigan (US)
  • Center for Biologics Evaluation and Research (US)
  • Department of Physiology, University of Michigan Medical School, Ann Arbor, MI 48109, USA.
Venue
Science
Published
1995-07-07
Volume
269
Issue
5220
Pages
81-83
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2032674547
Cited by
931
References
0
Citations by year
2026: 3 · 2025: 12 · 2024: 11 · 2023: 23 · 2022: 10 · 2021: 18 · 2020: 19 · 2019: 20 · 2018: 19 · 2017: 27 · 2016: 19 · 2015: 29 · 2014: 24 · 2013: 34 · 2012: 37
FWCI
16.70
Type
journal article
Language
en
Open access
closed
Locations
  • Science (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Cancer Institute (R01CA055652, CA-55652)
  • National Institute of Diabetes and Digestive and Kidney Diseases (R01DK034171, DK 34171)
Topics
  • Health Sciences › Medicine › Oncology › Cytokine Signaling Pathways and Interactions
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Keywords
STAT3, src oncogene, tyrosine phosphorylation, DNA-binding activity, oncogenic transformation, STAT signaling pathway, carcinogenesis, cytokine-induced gene expression
MeSH terms
Animals, Base Sequence, Cell Line, Transformed, Cell Transformation, Neoplastic, DNA, DNA-Binding Proteins, Growth Inhibitors, Interferon-gamma, Lymphokines, Molecular Sequence Data, Phosphorylation, Tyrosine, Signal Transduction, Trans-Activators, Oncogene Protein pp60(v-src), Interleukin-6, Phosphotyrosine, STAT3 Transcription Factor, Mice, Leukemia Inhibitory Factor

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