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Journal of Biochemistry Advance Access published online on July 17, 2008
Journal of Biochemistry, doi:10.1093/jb/mvn090
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© 2008 The Japanese Biochemical Society

JB Minireview

Biosynthesis, remodeling and functions of mammalian GPI-anchored proteins: recent progress.

Taroh Kinoshita1,2,3, Morihisa Fujita2,3 and Yusuke Maeda1,2,4

1WPI Immunology Frontier Research Center and 2Research Institute for Microbial Diseases, Osaka University, Osaka, Japan; 3CREST and 4PREST, Japan Society of Technology, Saitama, Japan.

Dr. Taroh Kinoshita, PhD, Department of Immunoregulation, Research Institute for Microbial Diseases, Osaka University, 3-1 Yamada-oka, Suita, Osaka 565-0871, Japan. Tel +81-6-6879-8328, Fax +81-6-6875-5233, E-mail tkinoshi{at}biken.osaka-u.ac.jp

Received June 10, 2008; Accepted July 1, 2008


  Abstract

More than 100 mammalian proteins are post-translationally modified by glycosylphosphatidylinositol (GPI) at their C-termini and are anchored to the cell surface membrane via the lipid portion. GPI-anchored proteins (GPI-APs) have various functions, such as hydrolytic enzymes, receptors, adhesion molecules, complement regulatory proteins and other immunologically important proteins. GPI-anchored proteins are mainly associated with membrane microdomains or membrane rafts enriched in sphingolipids and cholesterol. It is thought that association with membrane rafts is important for GPI-anchored proteins in signal transduction and other functions. Here, we review recent progress in studies on biosynthesis, remodeling and functions of mammalian GPI-APs.

Key Words: endoplasmic reticulum, fatty acid, glycosyltransferases, Golgi apparatus, post-translational modification


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