Titre
Ubiquitin-dependent degradation of multiple F-box proteins by an autocatalytic mechanism.
Type
article
Institution
UNIL/CHUV/Unisanté + institutions partenaires
Auteur(s)
Galan, J.M.
Auteure/Auteur
Peter, M.
Auteure/Auteur
Liens vers les unités
ISSN
0027-8424
Statut éditorial
Publié
Date de publication
1999
Volume
96
Numéro
16
Première page
9124
Dernière page/numéro d’article
9129
Langue
anglais
Résumé
Ubiquitin-dependent degradation of regulatory proteins controls many cellular processes, including cell cycle progression, morphogenesis, and signal transduction. Skp1p-cullin-F-box protein (SCF) complexes are ubiquitin ligases composed of a core complex including Skp1p, Cdc53p, one of multiple F-box proteins that are thought to provide substrate specificity to the complex, and the ubiquitin-conjugating enzyme, Cdc34p. It is not understood how SCF complexes are regulated and how physiological conditions alter their levels. Here we show that three F-box proteins, Grr1p, Cdc4p, and Met30p, are unstable components of the SCF, and are themselves degraded in a ubiquitin- and proteasome-dependent manner in vivo. Ubiquitination requires all the core components of the SCF and an intact F-box, suggesting that ubiquitination occurs within the SCF complex by an autocatalytic mechanism. Cdc4p and Grr1p are intrinsically unstable, and their steady-state levels did not fluctuate through the cell cycle. Taken together, our results suggest that ubiquitin-dependent degradation of F-box proteins allows rapid switching among multiple SCF complexes, thereby enabling cells to adapt quickly to changing physiological conditions and progression through different phases of the cell cycle.
Sujets
PID Serval
serval:BIB_12412
PMID
Open Access
Oui
Date de création
2007-11-19T11:03:34.791Z
Date de création dans IRIS
2025-05-20T13:30:24Z