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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Bibliographische Detailangaben
Hauptverfasser: Witkos, Tomasz M. (VerfasserIn) , Rhiel, Manuel (VerfasserIn) , Wieland, Felix T. (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 10 January 2019
In: Nature Communications
Year: 2019, Jahrgang: 10
ISSN:2041-1723
DOI:10.1038/s41467-018-08044-6
Online-Zugang:Verlag, Volltext: https://doi.org/10.1038/s41467-018-08044-6
Verlag, Volltext: https://www.nature.com/articles/s41467-018-08044-6
Volltext
Verfasserangaben: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
Beschreibung
Zusammenfassung: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.
Beschreibung:Gesehen am 08.04.2019
Beschreibung:Online Resource
ISSN:2041-1723
DOI:10.1038/s41467-018-08044-6