ArticleMolecular and cellular biology1997
Beta interferon and oncostatin M activate Raf-1 and mitogen-activated protein kinase through a JAK1-dependent pathway.
Article in Molecular and cellular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 108 citations in OpenAlex.
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- PML-II regulates ERK and AKT signal activation and IFNα-induced cell death.Cell communication and signaling : CCS · 2021Article
- Chaperone mediated detection of small molecule target binding in cells.Nature communications · 2020Article
- The barrier hypothesis and Oncostatin M: Restoration of epithelial barrier function as a novel therapeutic strategy for the treatment of type 2 inflammatory disease.Tissue barriers · 2017Review
- The enigmatic cytokine oncostatin m and roles in disease.ISRN inflammation · 2013Review
- Distinct evolution process among type I interferon in mammals.Protein & cell · 2013Article
- The interferon signaling network and transcription factor C/EBP-beta.Cellular & molecular immunology · 2007Review
- Type III interferon (IFN) induces a type I IFN-like response in a restricted subset of cells through signaling pathways involving both the Jak-STAT pathway and the mitogen-activated protein kinases.Journal of virology · 2007Article
- Intestinal Na+-K+-ATPase activity and molecular events downstream of interferon-gamma receptor stimulation.British journal of pharmacology · 2004Article
- Article
- JAK2 activates TFII-I and regulates its interaction with extracellular signal-regulated kinase.Molecular and cellular biology · 2001Article
- Kinases: positive and negative regulators of apoptosis.Leukemia · 2000Review
- Janus kinases: components of multiple signaling pathways.Oncogene · 2000Review
- Meaningful relationships: the regulation of the Ras/Raf/MEK/ERK pathway by protein interactions.The Biochemical journal · 2000Review
- Interferon-alpha2b reduces phosphorylation and activity of MEK and ERK through a Ras/Raf-independent mechanism.British journal of cancer · 2000Article
- Article
- Synergy between Raf and BCL2 in abrogating the cytokine dependency of hematopoietic cells.Leukemia · 2000Article
- Article
- A conditionally-active form of MEK1 results in autocrine tranformation of human and mouse hematopoietic cells.Oncogene · 2000Article
- Tyrosine phosphorylation of the proto-oncoprotein Raf-1 is regulated by Raf-1 itself and the phosphatase Cdc25A.Molecular and cellular biology · 1999Article
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14 authors at 6 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Activation of early response genes by interferons (IFNs) and other cytokines requires tyrosine phosphorylation of a family of transcription factors termed signal transducers and activators of transcription (Stats). The Janus family of tyrosine kinases (Jak1, Jak2, Jak3, and Tyk2) is required for cytokine-induced tyrosine phosphorylation and dimerization of the Stat proteins. In order for IFNs to stimulate maximal expression of Stat1alpha-regulated genes, phosphorylation of a serine residue in the carboxy terminus by mitogen-activated protein kinase (MAPK) is also required. In HeLa cells, both IFN-beta and oncostatin M (OSM) stimulated MAPK and Raf-1 enzyme activity, in addition to Stat1 and Stat3 tyrosine phosphorylation. OSM stimulation of Raf-1 correlated with GTP loading of Ras, whereas IFN-beta activation of Raf-1 was Ras independent. IFN-beta- and OSM-induced Raf-1 activity could be coimmunoprecipitated with either Jak1 or Tyk2. Furthermore, HeLa cells lacking Jak1 displayed no activation of STAT1alpha, STAT3, and Raf-1 by IFN-beta or OSM and also demonstrated no increase in the relative level of GTP-bound p21ras in response to OSM. The requirement for Jak1 for IFN-beta- and OSM-induced activation of Raf-1 was also seen in Jak1-deficient U4A fibrosarcoma cells. Interestingly, basal MAPK, but not Raf-1, activity was constitutively enhanced in Jak1-deficient HeLa cells. Transient expression of Jak1 in both Jak-deficient HeLa cells and U4A cells reconstituted the ability of IFN-beta and OSM to activate Raf-1 and decreased the basal activity of MAPK, while expression of a kinase-inactive form of the protein showed no effect. Moreover, U4A cells selected for stable expression of Jak1, or COS cells transiently expressing Jak1 or Tyk2 but not Jak3, exhibited enhanced Raf-1 activity. Therefore, it appears that Jak1 is required for Raf-1 activation by both IFN-beta and OSM. These results provide evidence for a link between the Jaks and the Raf/MAPK signaling pathways.
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