RGD Reference Report - PGAP2 is essential for correct processing and stable expression of GPI-anchored proteins. - Rat Genome Database

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PGAP2 is essential for correct processing and stable expression of GPI-anchored proteins.

Authors: Tashima, Y  Taguchi, R  Murata, C  Ashida, H  Kinoshita, T  Maeda, Y 
Citation: Tashima Y, etal., Mol Biol Cell. 2006 Mar;17(3):1410-20. Epub 2006 Jan 11.
RGD ID: 8553507
Pubmed: (View Article at PubMed) PMID:16407401
DOI: Full-text: DOI:10.1091/mbc.E05-11-1005

Biosynthesis of glycosylphosphatidylinositol-anchored proteins (GPI-APs) in the ER has been extensively studied, whereas the molecular events during the transport of GPI-APs from the ER to the cell surface are poorly understood. Here, we established new mutant cell lines whose surface expressions of GPI-APs were greatly decreased despite normal biosynthesis of GPI-APs in the ER. We identified a gene responsible for this defect, designated PGAP2 (for Post-GPI-Attachment to Proteins 2), which encoded a Golgi/ER-resident membrane protein. The low surface expression of GPI-APs was due to their secretion into the culture medium. GPI-APs were modified/cleaved by two reaction steps in the mutant cells. First, the GPI anchor was converted to lyso-GPI before exiting the trans-Golgi network. Second, lyso-GPI-APs were cleaved by a phospholipase D after transport to the plasma membrane. Therefore, PGAP2 deficiency caused transport to the cell surface of lyso-GPI-APs that were sensitive to a phospholipase D. These results demonstrate that PGAP2 is involved in the processing of GPI-APs required for their stable expression at the cell surface.


Gene Ontology Annotations    

Biological Process

Cellular Component

Objects Annotated

Genes (Rattus norvegicus)
Pgap2  (post-GPI attachment to proteins 2)

Additional Information