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MAPK1 — SMAD3

Pathways - manually collected, often from reviews:

• OpenBEL Selventa BEL large corpus: SMAD3 → MAPK1 (increases, MAPK1 Activity, SMAD3 Activity) Kretzschmar et al., Genes Dev 1999*
  Evidence: Ras acting via Erk MAP kinases causes phosphorylation of Smad2 and Smad3 at specific sites in the region linking the DNA-binding domain and the transcriptional activation domain.
• OpenBEL Selventa BEL large corpus: SMAD3 → MAPK1 (increases, SMAD3 Activity) Kretzschmar et al., Genes Dev 1999*
  Evidence: Ras acting via Erk MAP kinases causes phosphorylation of Smad2 and Smad3 at specific sites in the region linking the DNA-binding domain and the transcriptional activation domain.
• KEGG TGF-beta signaling pathway: MAPK1/MAPK3 → Complex of SMAD2-SMAD3-SMAD4 (protein-protein, inhibition)
  

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Biogrid Interaction: MAPK1 — SMAD3 (direct interaction, enzymatic study) Alarcón et al., Cell 2009
• IRef Biogrid Interaction: MAPK1 — SMAD3 (physical association, affinity chromatography technology) Brown et al., J Cell Biochem 2008
• IRef Hprd Interaction: MAPK1 — SMAD3 (in vivo) Kretzschmar et al., Genes Dev 1999*, Matsuura et al., Biochemistry 2005*
• IRef Hprd Interaction: MAPK1 — SMAD3 (in vitro) Kretzschmar et al., Genes Dev 1999*, Matsuura et al., Biochemistry 2005*
• IRef Intact Interaction: Complex of 48 proteins (physical association, tandem affinity purification) Brown et al., J Cell Biochem 2008

Text-mined interactions from Literome

Wrana et al., Science's STKE : signal transduction knowledge environment 2000 : In the cytosol, Smad translocation might be inhibited by mitogen activated protein kinase dependent phosphorylation, whereas in the nucleus Smads interact with a number of transcription factors that themselves are primary targets of other signaling pathways
Yang et al., Am J Pathol 2003 (Fibrosis) : Inhibition of Erk-1/2 activation by Mek kinase inhibitor PD98059 restored TGF-beta1 mediated Smad-2/3 nuclear accumulation and myofibroblast activation
Furukawa et al., Hepatology 2003 (Liver Cirrhosis) : In conclusion, p38 MAPK dependent Smad3 phosphorylation promoted extracellular matrix production in MFBs both in vitro and in vivo
Lee et al., Int J Oncol 2004 (Stomach Neoplasms) : In this study, we examined effects of cell adhesion status on the TGF-beta1 mediated Erk1/2 regulation, and roles of Smad proteins on the cell adhesion mediated effects, using a gastric carcinoma cell variant
Galliher et al., Cancer Res 2007 (MAP Kinase Signaling System...) : Interestingly, although the expression of Y284F-TbetaR-II mutants in breast cancer cells had no effect on TGF-beta stimulation of Smad2/3 , this TbetaR-II mutant completely abrogated p38 MAPK activation by TGF-beta
Daniel et al., J Cell Biochem 2007 : Using a specific inhibitor, we were also able to demonstrate an involvement of the p38 MAPK in the increase of Smad 3 phosphorylation following butyrate treatment, thus opening the view to further elucidate possible mechanisms mediating the upregulation of VDR expression following butyrate treatment in colon cancer cells
Zhao et al., Mol Cell Biochem 2008 (Fibrosis...) : Additionally, the inhibition of MAPK signaling had no effect on Smad activation elicited by chymase
Ivanova et al., American journal of physiology. Renal physiology 2008 : Transforming growth factor-beta1, on the other hand, induced early activation of Smad3 and its translocation to the nucleus, Erk1/2 phosphorylation, and early disruption of membrane E-cadherin localization
Schievenbusch et al., Biochem Biophys Res Commun 2009 (Fibrosis) : As previously shown, Erk1/2 phosphorylation results in Smad-linker phosphorylation, thereby antagonizing cellular signals induced by TGFbeta
Zhu et al., Prostate 2010 (MAP Kinase Signaling System) : These findings suggest a dual role for PHB as a downstream determinant of the cellular response to TGF-beta via Smad dependent pathway ( apoptosis ) and MAPK intracellular signaling ( survival )
Rodrigues Díez et al., PloS one 2010 (Fibrosis) : In cultured rat VSMCs, direct AngII/Smad pathway activation was mediated by p38 MAPK and ROCK activation
Ungefroren et al., Int J Oncol 2011 (Carcinoma, Pancreatic Ductal...) : Biochemically, dnSrc inhibition failed to block TGF-ß1/ALK5 induced activation of Smad2 and Smad3, but partially inhibited transcriptional activation of TGF-ß/Smad-responsive reporter genes, and effectively blocked basal and TGF-ß1 induced activation of p38 MAPK
Suwanabol et al., J Vasc Surg 2012 : Overexpression of the signaling protein Smad3 enhanced TGF-ß induced activation of ERK MAPK , whereas inhibition of Smad3 with a siRNA blocked ERK MAPK phosphorylation in response to TGF-ß ... Immunoprecipitation of phospho-ERK MAPK and blotting with Smad3 revealed a physical association, suggesting that activation of ERK MAPK by Smad3 requires a direct interaction ... In an in vivo rat carotid injury model, overexpression of Smad3 resulted in an increase in phosphorylated ERK MAPK as well as increased VSMC proliferation as measured by proliferating cell nuclear antigen
Fang et al., J Biol Chem 2012 (Breast Neoplasms...) : Disruption of Smad3 expression in mammary carcinoma cells blocked CCL2 induced cell survival and migration and partially reduced p42/44MAPK phosphorylation
Xu et al., Int J Oncol 2013 : p38 MAPK inhibitors ( SB 203580 ) can attenuate TGF-ß1 induced Smad3 expression and suppress the activation of smad3