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• W4367011167 abstract "Although hepatocyte growth factor (HGF) can act synergistically or antagonistically with transforming growth factor-β (TGF-β) signaling, molecular mechanism of their crosstalk remains unknown. Using antibodies which selectively distinguished receptor-regulated Smads (R-Smads) phosphorylated at linker regions from those at C-terminal regions, we herein showed that either HGF or TGF-β treatment of normal stomach-origin cells activated the JNK pathway, thereafter inducing endogenous R-Smads phosphorylation at linker regions. However, the phosphorylation at their C-terminal regions was not induced by HGF treatment. The activated JNK could directly phosphorylate R-Smads in vitro at the same sites that were phosphorylated in response to TGF-β or HGF in vivo. Thus, the linker regions of R-Smads were the common phosphorylation sites for HGF and TGF-β signaling pathways. The phosphorylation induced by simultaneous treatment with HGF and TGF-β allowed R-Smads to associate with Smad4 and to translocate into the nucleus. JNK pathway involved HGF and TGF-β-mediated infiltration potency since a JNK inhibitor SP600125 caused the reduction of invasive capacity induced by HGF and TGF-β signals. Moreover, a combined treatment with HGF and TGF-β led to a potent increase in plasminogen activator inhibitor type 1 transcriptional activity through Smad3 phosphorylation at the linker region. In contrast, HGF treatment reduced TGF-β-dependent activation of p15INK4B promoter, in which Smad3 phosphorylation at the C-terminal region was involved. In conclusion, HGF and TGF-β transmit the signals through JNK-mediated R-Smads phosphorylation at linker regions." @default.
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• W4367011167 date "2004-08-23" @default.
• W4367011167 modified "2023-10-18" @default.
• W4367011167 title "TGF-β and HGF transmit the signals through JNK-dependent Smad2/3 phosphorylation at the linker regions" @default.
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• W4367011167 doi "https://doi.org/10.1038/sj.onc.1207981" @default.
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