Phospho-R-Smad1/5/8 dissociates from the receptor complex

Stable Identifier
R-HSA-201453
Type
Reaction [dissociation]
Species
Homo sapiens
Compartment
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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).

Literature References
PubMed ID Title Journal Year
8893010 Partnership between DPC4 and SMAD proteins in TGF-beta signalling pathways

Lagna, G, Hata, A, Hemmati-Brivanlou, A, Massague, J

Nature 1996
9136927 The TGF-beta family mediator Smad1 is phosphorylated directly and activated functionally by the BMP receptor kinase

Kretzschmar, M, Liu, F, Hata, A, Doody, J, Massague, J

Genes Dev 1997
17356069 Endofin acts as a Smad anchor for receptor activation in BMP signaling

Shi, W, Chang, C, Nie, S, Xie, S, Wan, M, Cao, X

J Cell Sci 2007
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