IndraLab
Statements
"Smad4 is monoubiquitinated in lysine 519 in vivo, a modification that inhibits smad4 by impeding association with phospho-smad2. Fam reverts this negative modification, re-empowering smad4 function;control of smad4 is a good way to regulate bone formation. Fam and ectodermin/tif1gamma (ecto) were reported to respectively regulate the de-ubiquitination and ubiquitination of smad4."
reach
"However, our domain truncation data indicate that activated BRK interacts with an MH1 domain of SMAD4, which does not contain the SH3 recognition motif, suggesting that the Pro-X-X-Pro motif might be dispensable for SH3-mediated protein-protein interactions.Dupont et al. (34) previously found that a cycle of ubiquitination and deubiquitination regulates the function and protein-protein interaction of SMAD4: Ecto/TIF1γ-mediated monoubiquitination disassembles SMAD4 from the SMAD complex, while deubiquitination by FAM/USP9x allows SMAD4 to return to SMAD signaling pool."
"Smad4 is monoubiquitinated in lysine 519 in vivo, a modification that inhibits smad4 by impeding association with phospho-smad2. Fam reverts this negative modification, re-empowering smad4 function;control of smad4 is a good way to regulate bone formation. Fam and ectodermin/tif1gamma (ecto) were reported to respectively regulate the de-ubiquitination and ubiquitination of smad4."
"Smad4 is monoubiquitinated in lysine 519 in vivo, a modification that inhibits smad4 by impeding association with phospho-smad2. Fam reverts this negative modification, re-empowering smad4 function;control of smad4 is a good way to regulate bone formation. Fam and ectodermin/tif1gamma (ecto) were reported to respectively regulate the de-ubiquitination and ubiquitination of smad4."