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Cell. 2009 Oct 16;139(2):352-65. doi: 10.1016/j.cell.2009.08.040.

GPI glycan remodeling by PGAP5 regulates transport of GPI-anchored proteins from the ER to the Golgi.

Author information

1
Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan.

Abstract

Many eukaryotic proteins are attached to the cell surface via glycosylphosphatidylinositol (GPI) anchors. How GPI-anchored proteins (GPI-APs) are trafficked from the endoplasmic reticulum (ER) to the cell surface is poorly understood, but the GPI moiety has been postulated to function as a signal for sorting and transport. Here, we established mutant cells that were selectively defective in transport of GPI-APs from the ER to the Golgi. We identified a responsible gene, designated PGAP5 (post-GPI-attachment to proteins 5). PGAP5 belongs to a dimetal-containing phosphoesterase family and catalyzed the remodeling of the glycan moiety on GPI-APs. PGAP5 catalytic activity is a prerequisite for the efficient exit of GPI-APs from the ER. Our data demonstrate that GPI glycan acts as an ER-exit signal and suggest that glycan remodeling mediated by PGAP5 regulates GPI-AP transport in the early secretory pathway.

PMID:
19837036
DOI:
10.1016/j.cell.2009.08.040
[Indexed for MEDLINE]
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