Reactome | The phosphorylated R-SMAD:CO-SMAD complex rapidly translocat...

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created	[InstanceEdit:176006] Jassal, B, 2006-02-28 10:02:50
dbId	176008
displayName	The phosphorylated R-SMAD:CO-SMAD complex rapidly translocat...
literatureReference	[LiteratureReference:173516] The nuclear import function of Smad2 is masked by SARA and unmasked by TGFbeta-dependent phosphorylation [LiteratureReference:178148] Transforming growth factor-beta induces nuclear import of Smad3 in an importin-beta1 and Ran-dependent manner [LiteratureReference:178143] An extended bipartite nuclear localization signal in Smad4 is required for its nuclear import and transcriptional activity [LiteratureReference:9731118] A mechanism of repression of TGFbeta/ Smad signaling by oncogenic Ras
modified	[InstanceEdit:9732722] Orlic-Milacic, Marija, 2021-05-31
schemaClass	Summation
text	The phosphorylated R-SMAD:CO-SMAD complex rapidly translocates to the nucleus (Xu et al. 2000, Kurisaki et al. 2001, Xiao et al. 2003) where it binds directly to DNA and interacts with a plethora of transcription co-factors. Translocation of SMAD2 and SMAD3 to the nucleus is negatively regulated by ERK-mediated phosphorylation (Kretzschmar et al. 1999). Regulation of target gene expression can be either positive or negative. A classic example of a target gene of the pathway are the genes encoding for I-SMADs. Thus, TGF-beta/SMAD signaling induces the expression of the negative regulators of the pathway (negative feedback loop).

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