Reactome | Upon phosphorylation of the R-SMAD (SMAD2/3), the conformati...

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created	[InstanceEdit:176006] Jassal, B, 2006-02-28 10:02:50
dbId	176005
displayName	Upon phosphorylation of the R-SMAD (SMAD2/3), the conformati...
literatureReference	[LiteratureReference:177257] MADR2 is a substrate of the TGFbeta receptor and its phosphorylation is required for nuclear accumulation and signaling [LiteratureReference:175954] TGF-beta receptor-mediated signalling through Smad2, Smad3 and Smad4 [LiteratureReference:177255] Phosphorylation of Ser465 and Ser467 in the C terminus of Smad2 mediates interaction with Smad4 and is required for transforming growth factor-beta signaling [LiteratureReference:208376] Structural basis of heteromeric smad protein assembly in TGF-beta signaling
modified	[InstanceEdit:3656493] Orlic-Milacic, M, 2013-06-05
schemaClass	Summation
text	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).

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