1999年6月25日
GPI1 stabilizes an enzyme essential in the first step of glycosylphosphatidylinositol biosynthesis
Journal of Biological Chemistry
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- 巻
- 274
- 号
- 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
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- 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
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- 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