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

COPI is recruited to the membrane by binding to Arf GTPases. Here the authors find that GORAB, a trans-Golgi protein, promotes COPI recruitment by forming membrane domains that also contain the COPI-interacting protein Scyl1, which is required for efficient glycosylation of cargo proteins.

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Bibliographic Details
Main Authors: Witkos, Tomasz M. (Author) , Rhiel, Manuel (Author) , Wieland, Felix T. (Author)
Format: Article (Journal)
Language:English
Published: 10 January 2019
In: Nature Communications
Year: 2019, Volume: 10
ISSN:2041-1723
DOI:10.1038/s41467-018-08044-6
Online Access:Verlag, Volltext: https://doi.org/10.1038/s41467-018-08044-6
Verlag, Volltext: https://www.nature.com/articles/s41467-018-08044-6
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Author Notes:Tomasz M. Witkos, Wing Lee Chan, Merja Joensuu, Manuel Rhiel, Ed Pallister, Jane Thomas-Oates, A. Paul Mould, Alex A. Mironov, Christophe Biot, Yann Guerardel, Willy Morelle, Daniel Ungar, Felix T. Wieland, Eija Jokitalo, May Tassabehji, Uwe Kornak & Martin Lowe
Description
Summary:COPI is recruited to the membrane by binding to Arf GTPases. Here the authors find that GORAB, a trans-Golgi protein, promotes COPI recruitment by forming membrane domains that also contain the COPI-interacting protein Scyl1, which is required for efficient glycosylation of cargo proteins.
Item Description:Gesehen am 08.04.2019
Physical Description:Online Resource
ISSN:2041-1723
DOI:10.1038/s41467-018-08044-6