Phosphorylated SMAD2/3 dissociates from TGFBR

Stable Identifier
Reaction [dissociation]
Homo sapiens
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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
15350224 Structural basis of heteromeric smad protein assembly in TGF-beta signaling

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

Mol Cell 2004
8980228 MADR2 is a substrate of the TGFbeta receptor and its phosphorylation is required for nuclear accumulation and signaling

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

Cell 1996
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, Engstrom, U, ten Dijke, P, Heldin, CH, Wernstedt, C, Tamaki, K

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

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

EMBO J 1997
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