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S-Palmitoylation Sorts Membrane Cargo for Anterograde Transport in the Golgi

Authors :
Francesca Bottanelli
Frederic Pincet
Patrik Björkholm
James E. Rothman
Felix Rivera-Molina
Saad Syed
Moritz Hacke
Andreas M. Ernst
Derek Toomre
Omar Zaki
Zhiqun Xi
Aleksander A. Rebane
David Baddeley
Hong Zheng
Morven Graham
CSIRO: Digital Productivity and Services
Laboratoire de Physique Statistique de l'ENS (LPS)
Université Paris Diderot - Paris 7 (UPD7)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Fédération de recherche du Département de physique de l'Ecole Normale Supérieure - ENS Paris (FRDPENS)
École normale supérieure - Paris (ENS Paris)
Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Centre National de la Recherche Scientifique (CNRS)-École normale supérieure - Paris (ENS Paris)
Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Centre National de la Recherche Scientifique (CNRS)
Department of Physiology and Cellular Biophysics [New York, NY, USA]
Columbia University College of Physicians and Surgeons
Source :
Developmental Cell, Developmental Cell, Elsevier, 2018, 47 (4), pp.479-493.e7. ⟨10.1016/j.devcel.2018.10.024⟩
Publication Year :
2018
Publisher :
HAL CCSD, 2018.

Abstract

International audience; While retrograde cargo selection in the Golgi is known to depend on specific signals, it is unknown whether anterograde cargo is sorted, and anterograde signals have not been identified. We suggest here that S-palmitoylation of anterograde cargo at the Golgi membrane interface is an anterograde signal and that it results in concentration in curved regions at the Golgi rims by simple physical chemistry. The rate of transport across the Golgi of two S-palmitoylated membrane proteins is controlled by S-palmitoylation. The bulk of S-palmitoylated proteins in the Golgi behave analogously, as revealed by click chemistry-based fluorescence and electron microscopy. These palmitoylated cargos concentrate in the most highly curved regions of the Golgi membranes, including the fenestrated perimeters of cisternae and associated vesicles. A palmitoylated transmembrane domain behaves similarly in model systems.

Details

Language :
English
ISSN :
15345807
Database :
OpenAIRE
Journal :
Developmental Cell, Developmental Cell, Elsevier, 2018, 47 (4), pp.479-493.e7. ⟨10.1016/j.devcel.2018.10.024⟩
Accession number :
edsair.doi.dedup.....f918ecc034218ecce55d1492ea0bf1f5