| Peroxisome dependency of alkyl-containing GPI-anchor biosynthesis in the endoplasmic reticulum. | |
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MedLine Citation:
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PMID: 19815513 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Glycosylphosphatidylinositol-anchored proteins (GPI-APs) play various roles in cell-cell and cell-environment interactions. GPI is synthesized in the endoplasmic reticulum (ER) from phosphatidylinositol (PI) through step-wise reactions including transfers of monosaccharides and preassembled GPI is transferred en bloc to proteins. Cellular PI contains mostly diacyl glycerol and unsaturated fatty acid in the sn-2 position, whereas mammalian GPI-APs have mainly 1-alkyl-2-acyl PI and almost exclusively stearic acid, a saturated chain, at the sn-2 position. The latter characteristic is the result of fatty acid remodeling occurring in the Golgi, generating GPI-anchors compatible with raft membrane. The former characteristic is the result of diacyl to alkyl-acyl change occurring in the third GPI intermediate, glucosaminyl-inositolacylated-PI (GlcN-acyl-PI). Here we investigated the origin of the sn-1 alkyl-chain in GPI-APs. Using cell lines defective in the peroxisomal alkyl-phospholipid biosynthetic pathway, we demonstrated that generation of alkyl-containing GPI is dependent upon the peroxisomal pathway. We further demonstrated that in cells defective in the peroxisome pathway, the chain composition of the diacyl glycerol moiety in GlcN-acyl-PI is different from those in the first intermediate N-acetylglucosaminyl-PI and cellular PI, indicating that not only diacyl to alkyl-acyl change but also diacyl to diacyl change occurs in GlcN-acyl-PI. We therefore propose a biosynthetic step within GlcN-acyl-PI in which the diacyl glycerol (or diacyl phosphatidic acid) part is replaced by diradyl glycerol (or diradyl phosphatidic acid). These results highlight cooperation of three organelles, the ER, the Golgi, and the peroxisome, in the generation of the lipid portion of GPI-APs. |
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Authors:
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Noriyuki Kanzawa; Yusuke Maeda; Hideo Ogiso; Yoshiko Murakami; Ryo Taguchi; Taroh Kinoshita |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2009-10-07 |
Journal Detail:
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Title: Proceedings of the National Academy of Sciences of the United States of America Volume: 106 ISSN: 1091-6490 ISO Abbreviation: Proc. Natl. Acad. Sci. U.S.A. Publication Date: 2009 Oct |
Date Detail:
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Created Date: 2009-10-21 Completed Date: 2009-11-23 Revised Date: 2010-09-28 |
Medline Journal Info:
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Nlm Unique ID: 7505876 Medline TA: Proc Natl Acad Sci U S A Country: United States |
Other Details:
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Languages: eng Pagination: 17711-6 Citation Subset: IM |
Affiliation:
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Research Institute for Microbial Diseases, Osaka University, Suita-city, Osaka 565-0871, Japan. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Acyltransferases
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genetics,
metabolism Alkyl and Aryl Transferases / genetics, metabolism Animals CHO Cells Cricetinae Cricetulus Endoplasmic Reticulum / metabolism* Fatty Acids / chemistry, metabolism Genetic Complementation Test Glycosylphosphatidylinositols / biosynthesis*, chemistry* Golgi Apparatus / metabolism Humans Membrane Proteins / biosynthesis, chemistry Models, Biological Mutation Peroxisomes / metabolism* Recombinant Proteins / genetics, metabolism Spectrometry, Mass, Electrospray Ionization Transfection |
| Chemical | |
Reg. No./Substance:
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0/Fatty Acids; 0/Glycosylphosphatidylinositols; 0/Membrane Proteins; 0/Recombinant Proteins; EC 2.3.-/Acyltransferases; EC 2.3.1.42/glycerone-phosphate O-acyltransferase; EC 2.5.-/Alkyl and Aryl Transferases; EC 2.5.1.26/alkylglycerone-phosphate synthase |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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