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The type I TGF-beta receptor engages TRAF6 to activate TAK1 in a receptor kinase-independent manner.

Abstract：

:Transforming growth factor-beta (TGF-beta) is a multifunctional cytokine that regulates embryonic development and tissue homeostasis; however, aberrations of its activity occur in cancer. TGF-beta signals through its Type II and Type I receptors (TbetaRII and TbetaRI) causing phosphorylation of Smad proteins. TGF-beta-associated kinase 1 (TAK1), a member of the mitogen-activated protein kinase kinase kinase (MAPKKK) family, was originally identified as an effector of TGF-beta-induced p38 activation. However, the molecular mechanisms for its activation are unknown. Here we report that the ubiquitin ligase (E3) TRAF6 interacts with a consensus motif present in TbetaRI. The TbetaRI-TRAF6 interaction is required for TGF-beta-induced autoubiquitylation of TRAF6 and subsequent activation of the TAK1-p38/JNK pathway, which leads to apoptosis. TbetaRI kinase activity is required for activation of the canonical Smad pathway, whereas E3 activity of TRAF6 regulates the activation of TAK1 in a receptor kinase-independent manner. Intriguingly, TGF-beta-induced TRAF6-mediated Lys 63-linked polyubiquitylation of TAK1 Lys 34 correlates with TAK1 activation. Our data show that TGF-beta specifically activates TAK1 through interaction of TbetaRI with TRAF6, whereas activation of Smad2 is not dependent on TRAF6.

journal_name

Nat Cell Biol

journal_title

Nature cell biology

authors

Sorrentino A,Thakur N,Grimsby S,Marcusson A,von Bulow V,Schuster N,Zhang S,Heldin CH,Landström M

doi

10.1038/ncb1780

subject

Has Abstract

pub_date

2008-10-01 00:00:00

pages

1199-207

issue

10

eissn

1465-7392

issn

1476-4679

pii

ncb1780

journal_volume

10

pub_type

杂志文章

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