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.
Guardado en:
Autores principales: | 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 |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2019
|
Materias: | |
Acceso en línea: | https://doaj.org/article/dc9f0e13809c4552a229477915667865 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Golgi membrane protein Erd1 Is essential for recycling a subset of Golgi glycosyltransferases
por: Richa Sardana, et al.
Publicado: (2021) -
Characterization of glycosyl dioxolenium ions and their role in glycosylation reactions
por: Thomas Hansen, et al.
Publicado: (2020) -
Golgi organization is regulated by proteasomal degradation
por: Avital Eisenberg-Lerner, et al.
Publicado: (2020) -
Activation of STING requires palmitoylation at the Golgi
por: Kojiro Mukai, et al.
Publicado: (2016) -
DeepACSON automated segmentation of white matter in 3D electron microscopy
por: Ali Abdollahzadeh, et al.
Publicado: (2021)