IndraLab

"TGF? binds to TGF? receptor II on T cells, which leads to the recruitment of TGF? receptor I to the complex and activation of cytoplasmic transcription factors SMAD2 and SMAD3. "

"\"Smad proteins mediate signaling by transforming growth factor-beta (TGF-beta) 1 superfamily members (1-3). Upon binding of TGF-beta to cell surface complexes of type I and type II receptor serine/threonine kinases, the type II receptor phosphorylates the type I receptor, which further phosphorylates the receptor-regulated (R-) Smads, Smad2 and Smad3 (3). Phosphorylated R-Smads oligomerize with the common mediator (Co) Smad4 and accumulate in the nucleus where they regulate gene expression.\""

"Binding of TGF induces phosphorylation and activation of the TGF-beta R1 receptor by the TGF-beta R2 receptor."

"the SGK promoter contains consensus DNA elements for Smad and Fast-1 binding (hatched boxes labeled SMAD 3/4 and Fast-1 in figure 2) that are activated by TGF-beta receptor signaling, This protein is recruited to the TGF-beta receptors through its interaction with the SMAD anchor for receptor activation (SARA) protein. In response to TGF-beta signal, this protein is phosphorylated by the TGF-beta receptors. The phosphorylation induces the dissociation of this protein with SARA and the association with the family member SMAD4. The association with SMAD4 is important for the translocation of this protein into the nucleus, where it binds to target promoters and forms a transcription repressor complex with other cofactors. This protein can also be phosphorylated by activin type 1 receptor kinase, and mediates the signal from the activin. Alternatively spliced transcript variants encoding the same protein have been observed."

"the SGK promoter contains consensus DNA elements for Smad and Fast-1 binding (hatched boxes labeled SMAD 3/4 and Fast-1 in figure 2) that are activated by TGF-beta receptor signaling, This protein is recruited to the TGF-beta receptors through its interaction with the SMAD anchor for receptor activation (SARA) protein. In response to TGF-beta signal, this protein is phosphorylated by the TGF-beta receptors. The phosphorylation induces the dissociation of this protein with SARA and the association with the family member SMAD4. The association with SMAD4 is important for the translocation of this protein into the nucleus, where it binds to target promoters and forms a transcription repressor complex with other cofactors. This protein can also be phosphorylated by activin type 1 receptor kinase, and mediates the signal from the activin. Alternatively spliced transcript variants encoding the same protein have been observed."

"\"Smad proteins mediate signaling by transforming growth factor-beta (TGF-beta) 1 superfamily members (1-3). Upon binding of TGF-beta to cell surface complexes of type I and type II receptor serine/threonine kinases, the type II receptor phosphorylates the type I receptor, which further phosphorylates the receptor-regulated (R-) Smads, Smad2 and Smad3 (3). Phosphorylated R-Smads oligomerize with the common mediator (Co) Smad4 and accumulate in the nucleus where they regulate gene expression.\""

"TGF? binds to TGF? receptor II on T cells, which leads to the recruitment of TGF? receptor I to the complex and activation of cytoplasmic transcription factors SMAD2 and SMAD3."

"Further work revealed that TGF-R signaling (Massague and Wotton, 2000) was required for EMT, invasion in vitro, and metastasis in vivo,"