GPI glycan remodeling by PGAP5 regulates transport of GPI-anchored proteins from the ER to the Golgi.
Cell
; 139(2): 352-65, 2009 Oct 16.
Article
in En
| MEDLINE
| ID: mdl-19837036
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.
Full text:
1
Database:
MEDLINE
Main subject:
Polysaccharides
/
Phosphoric Diester Hydrolases
/
Endoplasmic Reticulum
/
Golgi Apparatus
Limits:
Animals
/
Humans
Language:
En
Year:
2009
Type:
Article