MISC

本文へのリンクあり
1999年6月25日

GPI1 stabilizes an enzyme essential in the first step of glycosylphosphatidylinositol biosynthesis

Journal of Biological Chemistry
  • Yeongjin Hong
  • ,
  • Kazuhito Ohishi
  • ,
  • Reika Watanabe
  • ,
  • Yuichi Endo
  • ,
  • Yusuke Maeda
  • ,
  • Taroh Kinoshita

274
26
開始ページ
18582
終了ページ
18588
記述言語
英語
掲載種別
DOI
10.1074/jbc.274.26.18582
出版者・発行元
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC

Attachment of glycosylphosphatidylinositol (GPI) is essential for the surface expression of many proteins. Biosynthesis of glycosylphosphatidylinositol is initiated by the transfer of N- acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol. In mammalian cells, this reaction is mediated by a complex of PIG-A, PIG-H, PIG- C, and GPI1. This complexity may be relevant for regulation and for usage of a particular phosphatidylinositol. However, the functions of the respective components have been unclear. Here we cloned the mouse GPI1 gene and disrupted it in F9 embryonal carcinoma cells. Disruption of the GPI1 gene caused a severe but not complete defect in the generation of glycosylphosphatldylinositol-anchored proteins, indicating some residual biosynthetic activity. A complex of PIG-A, PIG-H, and PIG-C decreased to a nearly undetectable level, whereas a complex of PIG-A and PIG-H was easily detected. A lack of GPI1 also caused partial decreases of PIG-C and PIG-H. Therefore, GPI1 stabilizes the enzyme by tying up PIG-C with a complex of PIG-A and PIG-H.

リンク情報
DOI
https://doi.org/10.1074/jbc.274.26.18582
CiNii Articles
http://ci.nii.ac.jp/naid/80011137771
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/10373468
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000081056700060&DestApp=WOS_CPL
Scopus
https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0033603587&origin=inward 本文へのリンクあり
Scopus Citedby
https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b&scp=0033603587&origin=inward
ID情報
  • DOI : 10.1074/jbc.274.26.18582
  • ISSN : 0021-9258
  • CiNii Articles ID : 80011137771
  • PubMed ID : 10373468
  • SCOPUS ID : 0033603587
  • Web of Science ID : WOS:000081056700060

エクスポート
BibTeX RIS