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MBC in Press, published online ahead of print January 11, 2006
Mol. Biol. Cell 10.1091/mbc.E05-11-1005

A more recent version of this article appeared on March 1, 2006
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Submitted on November 2, 2005
Revised on December 27, 2005
Accepted on January 4, 2005

PGAP2 Is Essential for Correct Processing and Stable Expression of GPI-anchored Proteins

Yuko Tashima,* Ryo Taguchi,{dagger} Chie Murata,{dagger} Hisashi Ashida,* Taroh Kinoshita,* and Yusuke Maeda*

*Department of Immunoregulation, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565-0871, Japan; {dagger}Department of Metabolome, Graduate School of Medicine, The University of Tokyo, Tokyo 113-0033, Japan

Monitoring Editor: Howard Riezman

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.

Address correspondence to: Taroh Kinoshita (tkinoshi{at}biken.osaka-u.ac.jp) or Yusuke Maeda (ymaeda{at}biken.osaka-u.ac.jp)




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