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Originally published as MBC in Press, 10.1091/mbc.E05-08-0743 on September 14, 2005

Vol. 16, Issue 11, 5236-5246, November 2005

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The Initial Enzyme for Glycosylphosphatidylinositol Biosynthesis Requires PIG-Y, a Seventh Component

Yoshiko Murakami *, Uamporn Siripanyaphinyo *, Yeongjin Hong {dagger}, Yuko Tashima *, Yusuke Maeda *, and Taroh Kinoshita *

* Department of Immunoregulation, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan; {dagger} Genomic Research Center for Enteropathogenic Bacteria and Department of Microbiology, Chonnam National University Medical School, Gwangju 501-746, Korea

Submitted August 10, 2005; Revised September 1, 2005; Accepted September 2, 2005
Monitoring Editor: Reid Gilmore

Biosynthesis of glycosylphosphatidylinositol (GPI) is initiated by an unusually complex GPI-N-acetylglucosaminyltransferase (GPI-GnT) consisting of at least six proteins. Here, we report that human GPI-GnT requires another component, termed PIG-Y, a 71 amino acid protein with two transmembrane domains. The Burkitt lymphoma cell line Daudi, severely defective in the surface expression of GPI-anchored proteins, was a null mutant of PIG-Y. A complex of six components was formed without PIG-Y. PIG-Y appeared to be directly associated with PIG-A, implying that PIG-Y is the key molecule that regulates GPI-GnT activity by binding directly to the catalytic subunit PIG-A. PIG-Y is probably homologous to yeast Eri1p, a component of GPI-GnT. We did not obtain evidence for a functional linkage between GPI-GnT and ras GTPases in mammalian cells as has been reported for yeast cells. A single transcript encoded PIG-Y and, to its 5' side, another protein PreY that has homologues in a wide range of organisms and is characterized by a conserved domain termed DUF343. These two proteins are translated from one mRNA by leaky scanning of the PreY initiation site.

This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E05–08–0743) on September 14, 2005.

Abbreviations used: GPI, glycosylphosphatidylinositol; GPI-GnT, GPI-N-acetylglucosaminyltransferase; GlcNAc, N-acetylglucosamine; GlcN, glucosamine; PI, phosphatidylinositol; IRES, internal ribosome entry site; DAF, decay accelerating factor.

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




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