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FEBS Lett. 2019 Aug 10. doi: 10.1002/1873-3468.13573. [Epub ahead of print]

Clustering in the Golgi apparatus governs sorting and function of GPI-APs in polarized epithelial cells.

Author information

1
Unité de Trafic Membranaire et Pathogénèse, Institut Pasteur, Paris, France.
2
Dipartimento di Medicina Molecolare e Biotecnologie Mediche, Università Federico II, Napoli, Italy.

Abstract

Glycosylphosphatidylinositol-anchored proteins (GPI-APs) are lipid-anchored proteins attached to the extracellular leaflet of the plasma membrane via a glycolipid anchor. GPI-APs are commonly associated with cholesterol- and sphingolipid-enriched membrane microdomains. These microdomains help regulating various biological activities, by segregating different proteins and lipids in (nanoscale) membrane compartments. In fibroblasts, GPI-APs form actin- and cholesterol-dependent nanoclusters directly at the plasma membrane (PM). By contrast, in polarized epithelial cells GPI-APs cluster in the Golgi apparatus, the major protein-sorting hub for the secretory pathway. Golgi clustering is required for the selective sorting of GPI-APs to the apical PM domain, but also regulates their organization and biological activities at the cell surface. In this review, we discuss recent advances in our understanding of the mechanism of GPI-AP sorting to the apical membrane. We focus on the roles of the protein moiety, lipids, and calcium ions in the regulation of the clustering of GPI-APs in the Golgi apparatus. This article is protected by copyright. All rights reserved.

KEYWORDS:

GPI-anchored proteins; Golgi complex; calcium; cholesterol; clustering; lipid microdomains; sorting

PMID:
31400147
DOI:
10.1002/1873-3468.13573

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