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Clustering in the Golgi apparatus governs sorting and function of GPI‐APs in polarized epithelial cells
Author(s) -
Lebreton Stéphanie,
Paladino Simona,
Zurzolo Chiara
Publication year - 2019
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13573
Subject(s) - microbiology and biotechnology , golgi apparatus , protein targeting , biology , membrane protein , chemistry , biochemistry , membrane , endoplasmic reticulum
Glycosylphosphatidylinositol‐anchored proteins (GPI‐APs) are lipid APs attached to the extracellular leaflet of the plasma membrane (PM) 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 PM. In 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 and lipids in the regulation of the clustering of GPI‐APs in the Golgi apparatus.