Phosphorylated SMAD2/3 dissociates from TGFBR

Stable Identifier
R-HSA-170850
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
8980228 MADR2 is a substrate of the TGFbeta receptor and its phosphorylation is required for nuclear accumulation and signaling

Macias-Silva, M, Abdollah, S, Hoodless, PA, Pirone, R, Attisano, L, Wrana, JL

Cell 1996
15350224 Structural basis of heteromeric smad protein assembly in TGF-beta signaling

Chacko, BM, Qin, BY, Tiwari, A, Shi, G, Lam, S, Hayward, LJ, De Caestecker, M, Lin, K

Mol Cell 2004
9346966 Phosphorylation of Ser465 and Ser467 in the C terminus of Smad2 mediates interaction with Smad4 and is required for transforming growth factor-beta signaling

Souchelnytskyi, S, Tamaki, K, Engstrom, U, Wernstedt, C, ten Dijke, P, Heldin, CH

J Biol Chem 1997
9311995 TGF-beta receptor-mediated signalling through Smad2, Smad3 and Smad4

Nakao, A, Souchelnytskyi, S, Kawabata, M, Ishisaki, A, Oeda, E, Tamaki, K, Hanai, J, Heldin, CH, Miyazono, K, ten Dijke, P

EMBO J 1997
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