Publication: Trafficking of glycosylphosphatidylinositol anchored proteins from the endoplasmic reticulum to the cell surface.
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Identifiers
Date
2016-03
Authors
Muñiz, Manuel
Riezman, Howard
Advisors
Journal Title
Journal ISSN
Volume Title
Publisher
Elsevier Inc.
Abstract
In eukaryotes, many cell surface proteins are attached to the plasma membrane via a glycolipid glycosylphosphatidylinositol (GPI) anchor. GPI-anchored proteins (GPI-APs) receive the GPI anchor as a conserved posttranslational modification in the lumen of the endoplasmic reticulum (ER). After anchor attachment, the GPI anchor is structurally remodeled to function as a transport signal that actively triggers the delivery of GPI-APs from the ER to the plasma membrane, via the Golgi apparatus. The structure and composition of the GPI anchor confer a special mode of interaction with membranes of GPI-APs within the lumen of secretory organelles that lead them to be differentially trafficked from other secretory membrane proteins. In this review, we examine the mechanisms by which GPI-APs are selectively transported through the secretory pathway, with special focus on the recent progress made in their actively regulated export from the ER and the trans-Golgi network.
Description
MeSH Terms
Animals
Endoplasmic Reticulum
Glycosylphosphatidylinositols
Humans
Membrane Proteins
Protein Transport
trans-Golgi Network
Endoplasmic Reticulum
Glycosylphosphatidylinositols
Humans
Membrane Proteins
Protein Transport
trans-Golgi Network
DeCS Terms
Proteínas ancladas a GPI
Remodelado del anclaje GPI
Retículo endoplásmico
Aparato de Golgi
Vía secretora
Tráfico de membrana
Remodelado del anclaje GPI
Retículo endoplásmico
Aparato de Golgi
Vía secretora
Tráfico de membrana
CIE Terms
Keywords
glycolipid anchor remodeling, lipid-based sorting, p24 complex
Citation
Muñiz M, Riezman H. Trafficking of glycosylphosphatidylinositol anchored proteins from the endoplasmic reticulum to the cell surface. J Lipid Res. 2016 Mar;57(3):352-60.