O-GlcNAc transferase catalyzes site-specific proteolysis of HCF-1.

Détails

ID Serval
serval:BIB_AD874A25FC24
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
O-GlcNAc transferase catalyzes site-specific proteolysis of HCF-1.
Périodique
Cell
Auteur(s)
Capotosti F., Guernier S., Lammers F., Waridel P., Cai Y., Jin J., Conaway J.W., Conaway R.C., Herr W.
ISSN
1097-4172 (Electronic)
ISSN-L
0092-8674
Statut éditorial
Publié
Date de publication
2011
Volume
144
Numéro
3
Pages
376-388
Langue
anglais
Résumé
The human epigenetic cell-cycle regulator HCF-1 undergoes an unusual proteolytic maturation process resulting in stably associated HCF-1(N) and HCF-1(C) subunits that regulate different aspects of the cell cycle. Proteolysis occurs at six centrally located HCF-1(PRO)-repeat sequences and is important for activation of HCF-1(C)-subunit functions in M phase progression. We show here that the HCF-1(PRO) repeat is recognized by O-linked β-N-acetylglucosamine transferase (OGT), which both O-GlcNAcylates the HCF-1(N) subunit and directly cleaves the HCF-1(PRO) repeat. Replacement of the HCF-1(PRO) repeats by a heterologous proteolytic cleavage signal promotes HCF-1 proteolysis but fails to activate HCF-1(C)-subunit M phase functions. These results reveal an unexpected role of OGT in HCF-1 proteolytic maturation and an unforeseen nexus between OGT-directed O-GlcNAcylation and proteolytic maturation in HCF-1 cell-cycle regulation.
Mots-clé
Amino Acid Sequence, Cell Cycle, Glycosylation, Host Cell Factor C1/chemistry, Host Cell Factor C1/genetics, Humans, Molecular Sequence Data, Mutation, N-Acetylglucosaminyltransferases/metabolism, Protein Processing, Post-Translational, Protein Subunits/metabolism, Sequence Alignment
Pubmed
Web of science
Open Access
Oui
Création de la notice
28/03/2011 11:30
Dernière modification de la notice
20/08/2019 16:17
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