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10.1194/jlr.R062760

http://scihub22266oqcxt.onion/10.1194/jlr.R062760
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C4767001!4767001!26450970
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suck abstract from ncbi


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pmid26450970      J+Lipid+Res 2016 ; 57 (3): 352-60
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  • Trafficking of glycosylphosphatidylinositol anchored proteins from the endoplasmic reticulum to the cell surface #MMPMID26450970
  • Muņiz M; Riezman H
  • J Lipid Res 2016[Mar]; 57 (3): 352-60 PMID26450970show ga
  • 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.
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