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Stable Cell Surface Expression of GPI ‐Anchored Proteins, but not Intracellular Transport, Depends on their Fatty Acid Structure
Author(s) -
Jaensch Nina,
Corrêa Ivan R.,
Watanabe Reika
Publication year - 2014
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/tra.12224
Subject(s) - biology , endocytosis , microbiology and biotechnology , endosome , biochemistry , fatty acid , sphingolipid , lipid droplet , intracellular , lipid signaling , adipocyte protein 2 , lipid metabolism , transport protein , cell , receptor
The importance of two saturated fatty acids within the phosphatidylinositol of glycosylphosphatidylinositol‐anchored proteins ( GPI‐APs ) was examined. The lipid remodeling reaction that replaces unsaturated fatty acid with saturated fatty acid in the GPI lipid moiety was not required for efficient Golgi‐to‐plasma membrane transport, endocytosis via GPI‐enriched early endosomal compartment ( GEEC )/ clathrin‐independent carrier ( CLIC ) pathway and further sorting to the recycling endosome. In contrast, more than 60% of unremodeled GPI‐APs carrying an unsaturated fatty acid were specifically released from cell surface during cholesterol extraction, highlighting the essential role of remodeling for stable membrane association under membrane lipid perturbation.