The SMAD protein family is currently found in 9 species, called SMAD1-9, which have been found to be involved in the signal transduction of TGF-BETA. It is a downstream signal transduction molecule, including receptor type, common medium type, and inhibitory type. 3 categories. The main steps of signal transduction in the TGF-BETA family are: 1. The TGF-BETA factor (ligand) interacts with receptors with serine/threonine kinase activity on the corresponding membrane (ie, Tbeta receptors I and II). Phosphorylation activates receptor II, and then reactivates receptor II to activate receptor I to form a complex; 2. Intracellular signal transduction of TGF-BETA family: formation of SMAD-mediated protein after receptor activation Heterologous oligomers transmit TGF-BETA family signals to the nucleus; 3. Intranuclear signal transduction of the TGF-BETA family: nuclear SMAD oligomers act as transcription factors directly with DNA, or with other transcription factors and activation Factor interactions induce a transcriptional response to TGF-BETA signaling and regulate transcription of the corresponding target gene. The SMAD family is a single-chain polypeptide with a molecular weight of 40-60 kD. It has three basic functional regions: a conserved amino-terminal MH1 region and a carboxy-terminal MH2 region, with a variable linkage region in the middle, and a proline-rich hinge region in the junction region. Multiple phosphorylation sites, including the MAP kinase phosphorylation site, are phosphorylated by ERK, which, after phosphorylation, inhibits nuclear transfer of the SMAD protein and is a negative regulatory region of SMAD. TGF0-BETA itself is a stimulating factor for SMAD, and SMAD1, 2, 3, 4, etc. can be activated by it. In addition, SARA (an anchoring protein) acts as a bridge between SMAD2, 3 and TGF-BETA receptors and can also participate in and promote its binding to receptors.
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Amino compound
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