TGFBR2 phosphorylates TGFBR1

Stable Identifier
Reaction [transition]
Homo sapiens
Type II receptor phosphorylates type I receptor
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Formation of the hetero-tetrameric TGF-beta-1 receptor complex induces receptor rotation, so that TGFBR2 and TGFBR1 cytoplasmic kinase domains face each other in a catalytically favourable configuration. The constitutively active type II receptor kinase (which auto-phosphorylates in the absence of ligand), trans-phosphorylates specific serine residues at the conserved Gly-Ser-rich juxtapositioned domain (GS domain) of the type I receptor (Wrana et al. 1994, Souchelnytskyi et al. 1996).

In addition to phosphorylation, TGFBR1 may also be sumoylated in response to TGF-beta-1 stimulation. Sumoylation enhances TGFBR1 function by facilitating recruitment and phosphorylation of SMAD3 (Kang et al. 2008).

Literature References
PubMed ID Title Journal Year
8947046 Phosphorylation of Ser165 in TGF-beta type I receptor modulates TGF-beta1-induced cellular responses

Miyazono, K, Souchelnytskyi, S, ten Dijke, P, Heldin, CH

EMBO J 1996
8047140 Mechanism of activation of the TGF-beta receptor

Massague, J, Wrana, JL, Wieser, R, Attisano, L, Ventura, F

Nature 1994
18469808 The type I TGF-beta receptor is covalently modified and regulated by sumoylation

Derynck, R, Kang, JS, Akhurst, RJ, Saunier, EF

Nat. Cell Biol. 2008
Catalyst Activity

transforming growth factor beta receptor activity, type II of TGFB1:TGFBR2:TGFBR1 [plasma membrane]

Orthologous Events
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