Recognition of a glycosylation substrate by the O-GlcNAc transferase TPR repeats.

Détails

Ressource 1Télécharger: rsob-7-170078.pdf (794.11 [Ko])
Etat: Public
Version: Final published version
ID Serval
serval:BIB_E1EF6AEE1CB4
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Recognition of a glycosylation substrate by the O-GlcNAc transferase TPR repeats.
Périodique
Open biology
Auteur⸱e⸱s
Rafie K., Raimi O., Ferenbach A.T., Borodkin V.S., Kapuria V., van Aalten DMF
ISSN
2046-2441 (Electronic)
ISSN-L
2046-2441
Statut éditorial
Publié
Date de publication
06/2017
Peer-reviewed
Oui
Volume
7
Numéro
6
Pages
170078
Langue
anglais
Notes
Publication types: Journal Article
Publication Status: ppublish
Résumé
O-linked <i>N</i> -acetylglucosamine (O-GlcNAc) is an essential and dynamic post-translational modification found on hundreds of nucleocytoplasmic proteins in metazoa. Although a single enzyme, O-GlcNAc transferase (OGT), generates the entire cytosolic O-GlcNAc proteome, it is not understood how it recognizes its protein substrates, targeting only a fraction of serines/threonines in the metazoan proteome for glycosylation. We describe a trapped complex of human OGT with the C-terminal domain of TAB1, a key innate immunity-signalling O-GlcNAc protein, revealing extensive interactions with the tetratricopeptide repeats of OGT. Confirmed by mutagenesis, this interaction suggests that glycosylation substrate specificity is achieved by recognition of a degenerate sequon in the active site combined with an extended conformation C-terminal of the O-GlcNAc target site.
Mots-clé
Adaptor Proteins, Signal Transducing/drug effects, Adaptor Proteins, Signal Transducing/genetics, Amino Acid Sequence, Glycosylation, Humans, N-Acetylglucosaminyltransferases/genetics, N-Acetylglucosaminyltransferases/metabolism, Sequence Alignment, Substrate Specificity, Tetratricopeptide Repeat/genetics, Tetratricopeptide Repeat/physiology, O-GlcNAc, O-GlcNAc transferase, glycosylation, signalling, substrate recognition
Pubmed
Web of science
Open Access
Oui
Création de la notice
27/07/2017 13:32
Dernière modification de la notice
20/08/2019 17:05
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