Phosphorylated SMAD2/3 dissociates from TGFBR
收藏reactome.org2025-01-15 收录
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Upon phosphorylation of the R-SMAD (SMAD2/3), the conformation of the C-terminal (MH2) domain of the R-SMAD changes, lowering its affinity for the type I receptor and ZFYVE9 (SARA). As a result, the phosphorylated R-SMAD dissociates from the activated receptor complex (TGFBR).
在R-SMAD(SMAD2/3)磷酸化之后,其C端(MH2)结构域的构象发生改变,从而降低其对I型受体和ZFYVE9(SARA)的结合亲和力。因此,磷酸化的R-SMAD会从激活的受体复合物(TGFBR)中解离出来。
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