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Dev Cell. 2018 Nov 19;47(4):479-493.e7. doi: 10.1016/j.devcel.2018.10.024.

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

Author information

1
Department of Cell Biology, Yale School of Medicine, New Haven, CT 06520, USA. Electronic address: andreas.ernst@yale.edu.
2
Department of Cell Biology, Yale School of Medicine, New Haven, CT 06520, USA.
3
Department of Cell Biology, Yale School of Medicine, New Haven, CT 06520, USA; Laboratoire de Physique Statistique, Ecole Normale Supérieure, PSL Research University, Université Paris Diderot Sorbonne Paris Cité, Sorbonne Universités UPMC Univ, CNRS, Paris, France.
4
Department of Cell Biology, Yale School of Medicine, New Haven, CT 06520, USA. Electronic address: james.rothman@yale.edu.

Abstract

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.

KEYWORDS:

DHHC; Golgi; S-palmitoylation; cargo sorting; trafficking

PMID:
30458139
PMCID:
PMC6251505
[Available on 2019-11-19]
DOI:
10.1016/j.devcel.2018.10.024
[Indexed for MEDLINE]

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