Inducible degradation of IkappaBalpha by the proteasome requires interaction with the F-box protein h-betaTrCP

M Kroll, F Margottin, A Kohl, P Renard, H Durand, J P Concordet, F Bachelerie, F Arenzana-Seisdedos, R Benarous

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Résumé

Activation of NF-kappaB transcription factors requires phosphorylation and ubiquitin-proteasome-dependent degradation of IkappaB proteins. We provide evidence that a human F-box protein, h-betaTrCP, a component of Skp1-Cullin-F-box protein (SCF) complexes, a new class of E3 ubiquitin ligases, is essential for inducible degradation of IkappaBalpha. betaTrCP associates with Ser32-Ser36 phosphorylated, but not with unmodified IkappaBalpha or Ser32-Ser36 phosphorylation-deficient mutants. Expression of a F-box-deleted betaTrCP inhibits IkappaBalpha degradation, promotes accumulation of phosphorylated Ser32-Ser36 IkappaBalpha, and prevents NF-kappaB-dependent transcription. Our findings indicate that betaTrCP is the adaptor protein required for IkappaBalpha recognition by the SCFbetaTrCP E3 complex that ubiquitinates IkappaBalpha and makes it a substrate for the proteasome.
langue originaleAnglais
Pages (de - à)7941-5
Nombre de pages5
journalThe Journal of Biological Chemistry
Volume274
Numéro de publication12
Etat de la publicationPublié - 19 mars 1999

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