Reactome | Phosphorylated SMAD2/3 dissociates from TGFBR

Phosphorylated SMAD2/3 dissociates from TGFBR

Stable Identifier

R-HSA-170850

Type

Reaction [dissociation]

Species

Homo sapiens

Compartment

early endosome

ReviewStatus

5/5

Locations in the PathwayBrowser

Expand all

General

SBML | | PDF

SVG | | PPTX | SBGN

Phosphorylated SMAD2/3 dissociates from TGFBR

Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

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