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Title: Trafficking of glycosylphosphatidylinositol anchored proteins from the endoplasmic reticulum to the cell surface.
Authors: Muñiz, Manuel
Riezman, Howard
Keywords: glycolipid anchor remodeling;lipid-based sorting;p24 complex
metadata.dc.subject.mesh: Animals
Endoplasmic Reticulum
Membrane Proteins
Protein Transport
trans-Golgi Network
Issue Date: 8-Oct-2015
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.
metadata.dc.identifier.doi: 10.1194/jlr.R062760
Appears in Collections:Producción 2020

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