Molecular Biology of the Cell Sign up for new MBC in Press e-TOCs!

Home Help [Feedback] [For Subscribers] [Archive] [Search] --
QUICK SEARCH:   [advanced]


     

MBC in Press, published online ahead of print September 14, 2005
Mol. Biol. Cell 10.1091/mbc.E05-08-0743

A more recent version of this article appeared on November 1, 2005
This Article
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
E05-08-0743v1
16/11/5236    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Murakami, Y.
Right arrow Articles by Kinoshita, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Murakami, Y.
Right arrow Articles by Kinoshita, T.

Submitted on August 10, 2005
Revised on September 1, 2005
Accepted on September 2, 2005

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

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.

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




This article has been cited by other articles:


Home page
 J. Lipid Res.Home page
P. Orlean and A. K. Menon
Thematic review series: Lipid Posttranslational Modifications. GPI anchoring of protein in yeast and mammalian cells, or: how we learned to stop worrying and love glycophospholipids
J. Lipid Res., May 1, 2007; 48(5): 993 - 1011.
[Abstract] [Full Text] [PDF]

Home page
 ASH Education BookHome page
R. A. Brodsky
New Insights into Paroxysmal Nocturnal Hemoglobinuria
Hematology, January 1, 2006; 2006(1): 24 - 28.
[Abstract] [Full Text] [PDF]


Home Help [Feedback] [For Subscribers] [Archive] [Search] --
Copyright © 2005 by The American Society for Cell Biology. Terms of copyright protection, warranties, and disclaimers.