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Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGF beta receptor for degradation.

Abstract：

:Ubiquitin-mediated proteolysis regulates the activity of diverse receptor systems. Here, we identify Smurf2, a C2-WW-HECT domain ubiquitin ligase and show that Smurf2 associates constitutively with Smad7. Smurf2 is nuclear, but binding to Smad7 induces export and recruitment to the activated TGF beta receptor, where it causes degradation of receptors and Smad7 via proteasomal and lysosomal pathways. IFN gamma, which stimulates expression of Smad7, induces Smad7-Smurf2 complex formation and increases TGF beta receptor turnover, which is stabilized by blocking Smad7 or Smurf2 expression. Furthermore, Smad7 mutants that interfere with recruitment of Smurf2 to the receptors are compromised in their inhibitory activity. These studies thus define Smad7 as an adaptor in an E3 ubiquitin-ligase complex that targets the TGF beta receptor for degradation.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Kavsak P,Rasmussen RK,Causing CG,Bonni S,Zhu H,Thomsen GH,Wrana JL

doi

10.1016/s1097-2765(00)00134-9

subject

Has Abstract

pub_date

2000-12-01 00:00:00

pages

1365-75

issue

6

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(00)00134-9

journal_volume

6

pub_type

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