TGF-β induces assembly of a Smad2–Smurf2 ubiquitin ligase complex that targets SnoN for degradation
Author: ["Shirin Bonni","Hong-Rui Wang","Carrie G. Causing","Peter Kavsak","Shannon L. Stroschein","Kunxin Luo","Jeffrey L. Wrana"]
Publication: Nature Cell Biology
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Abstract
The receptor-regulated Smad proteins are essential intracellular mediators of signal transduction by the transforming growth factor-β (TGF-β) superfamily of growth factors and are also important as regulators of gene transcription. Here we describe a new role for TGF-β-regulated Smad2 and Smad3 as components of a ubiquitin ligase complex. We show that in the presence of TGF-β signalling, Smad2 interacts through its proline-rich PPXY motif with the tryptophan-rich WW domains of Smurf2, a recently identified E3 ubiquitin ligases. TGF-β also induces the association of Smurf2 with the transcriptional co-repressor SnoN and we show that Smad2 can function to mediate this interaction. This allows Smurf2 HECT domain to target SnoN for ubiquitin-mediated degradation by the proteasome. Thus, stimulation by TGF-β can induce the assembly of a Smad2–Smurf2 ubiquitin ligase complex that functions to target substrates for degradation.
Cite this article
Bonni, S., Wang, HR., Causing, C. et al. TGF-β induces assembly of a Smad2–Smurf2 ubiquitin ligase complex that targets SnoN for degradation. Nat Cell Biol 3, 587–595 (2001). https://doi.org/10.1038/35078562
