Titre :

GORAB scaffolds COPI at the trans-Golgi for efficient enzyme recycling and correct protein glycosylation

Auteur(s) :

Witkos, Tomasz M [Auteur]
University of Manchester Institute of Science and Technology [UMIST]
Chan, Wing Lee [Auteur]
Joensuu, Merja [Auteur]
Helsingin yliopisto = Helsingfors universitet = University of Helsinki
Rhiel, Manuel [Auteur]
Universität Heidelberg [Heidelberg] = Heidelberg University
Pallister, Ed [Auteur]
Department of Chemistry [York, UK]
Thomas-Oates, Jane [Auteur]
Department of Chemistry [York, UK]
Mould, A Paul [Auteur]
University of Manchester Institute of Science and Technology [UMIST]
Mironov, Alex A [Auteur]
University of Manchester Institute of Science and Technology [UMIST]
Biot, Christophe [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Guerardel, Yann [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Morelle, Willy [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Ungar, Daniel [Auteur]
Department of Biology [York]
Wieland, Felix T [Auteur]
Universität Heidelberg [Heidelberg] = Heidelberg University
Jokitalo, Eija [Auteur]
Helsingin yliopisto = Helsingfors universitet = University of Helsinki
Tassabehji, May [Auteur]
University of Manchester Institute of Science and Technology [UMIST]
Kornak, Uwe [Auteur]
Lowe, Martin [Auteur]
University of Manchester Institute of Science and Technology [UMIST]

Titre de la revue :

Nature Communications

Nom court de la revue :

Nat Commun

Numéro :

10

Pagination :

127

Date de publication :

2019-01-10

ISSN :

2041-1723

Mot(s)-clé(s) en anglais :

Bone Diseases
Carrier Proteins
Cells
Cultured
Coat Protein Complex I
Dwarfism
Enzymes
Glycosylation
Golgi Apparatus
Golgi Matrix Proteins
HEK293 Cells
HeLa Cells
Humans
Mutation
Protein Binding
Protein Transport
RNA Interference
Skin Diseases
Genetic
Transcription Factors

Discipline(s) HAL :

Sciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire/Biologie structurale [q-bio.BM]

Résumé en anglais : [en]

COPI is a key mediator of protein trafficking within the secretory pathway. COPI is recruited to the membrane primarily through binding to Arf GTPases, upon which it undergoes assembly to form coated transport intermediates ...
Lire la suite >COPI is a key mediator of protein trafficking within the secretory pathway. COPI is recruited to the membrane primarily through binding to Arf GTPases, upon which it undergoes assembly to form coated transport intermediates responsible for trafficking numerous proteins, including Golgi-resident enzymes. Here, we identify GORAB, the protein mutated in the skin and bone disorder gerodermia osteodysplastica, as a component of the COPI machinery. GORAB forms stable domains at the trans-Golgi that, via interactions with the COPI-binding protein Scyl1, promote COPI recruitment to these domains. Pathogenic GORAB mutations perturb Scyl1 binding or GORAB assembly into domains, indicating the importance of these interactions. Loss of GORAB causes impairment of COPI-mediated retrieval of trans-Golgi enzymes, resulting in a deficit in glycosylation of secretory cargo proteins. Our results therefore identify GORAB as a COPI scaffolding factor, and support the view that defective protein glycosylation is a major disease mechanism in gerodermia osteodysplastica.Lire moins >

Audience :

Non spécifiée

Établissement(s) :

Université de Lille
CNRS

Collections :

• Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576

Date de dépôt :

2020-11-18T14:02:08Z
2020-11-25T07:02:42Z