IndraLab

Statements

PTK6 binds SMAD4. 8 / 8
| 4 4
sparser
"Our search for signaling pathways regulated by breast tumor kinase (BRK), a nonreceptor protein tyrosine kinase that is up-regulated in ~80% of invasive ductal breast tumors, led us to find that BRK competitively binds and phosphorylates SMAD4 and regulates transforming growth factor–β/SMAD4 signaling pathway."
31681835
sparser
"We have shown that activated BRK interacts with SMAD4 and colocalizes with SMAD4 in the cytosol of live cells."
31681835
reach
"The extensive proteomics data from the same study revealed that PTK6/phosphorylated-SMAD4 interacts with the core subunits of chromatin remodeling and histone deacetylase NuRD complex and forms a PTK6- SMAD4-NuRD complex."
37147457
sparser
"These APMS experiments hence confirmed the conclusion from the coimmunoprecipitation experiments: BRK interacts with SMAD4."
31681835
reach
"Recently, we also discovered that protein tyrosine kinase 6 (PTK6) (also known as breast tumor kinase, BRK) interacts with SMAD2/3/4 and phosphorylates SMAD4, which alters TGF-β/SMAD signaling and increases the metastatic potential of breast cancer cells [19]."
37147457
reach
"In contrast, ΔSH3-BRK did not coprecipitate with GFP-SMAD4, suggesting that the SH3 domain is necessary for BRK/SMAD4 interaction (Fig. 2D)."
31681835
sparser
"We have found that activated BRK competitively binds and phosphorylates SMAD4 and regulates TGF-β/SMAD signaling pathways."
31681835
reach
"We have found that activated BRK competitively binds and phosphorylates SMAD4 and regulates TGF-β/SMAD signaling pathways."
31681835