2006年12月
PER1 is required for GPI-phospholipase A(2) activity and involved in lipid remodeling of GPI-anchored proteins
MOLECULAR BIOLOGY OF THE CELL
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- ,
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- 巻
- 17
- 号
- 12
- 開始ページ
- 5253
- 終了ページ
- 5264
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1091/mbc.E06-08-0715
- 出版者・発行元
- AMER SOC CELL BIOLOGY
Glycosylphoshatidylinositol (GPI) anchors are remodeled during their transport to the cell surface. Newly synthesized proteins are transferred to a GPI anchor, consisting of diacylglycerol with conventional C16 and C18 fatty acids, whereas the lipid moiety in mature GPI-anchored proteins is exchanged to either diacylglycerol containing a C26:0 fatty acid in the sn-2 position or ceramide in Saccharomyces cerevisiae. Here, we report on PER1, a gene encoding a protein that is required for the GPI remodeling pathway. We found that GPI-anchored proteins could not associate with the detergent-resistant membranes in per1 Delta cells. In addition, the mutant cells had a defect in the lipid remodeling from normal phosphatidylinositol (PI) to a C26 fatty acid-containing PI in the GPI anchor. In vitro analysis showed that PER1 is required for the production of lyso-GPI, suggesting that Per1p possesses or regulates the GPI-phospholipase A(2) activity. We also found that human PERLD1 is a functional homologue of PER1. Our results demonstrate for the first time that PERI encodes an evolutionary conserved component of the GPI anchor remodeling pathway, highlighting the close connection between the lipid remodeling of GPI and raft association of GPI-anchored proteins.
- リンク情報
- ID情報
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- DOI : 10.1091/mbc.E06-08-0715
- ISSN : 1059-1524
- eISSN : 1939-4586
- PubMed ID : 17021251
- Web of Science ID : WOS:000242653200027