Document Detail


Peroxisome dependency of alkyl-containing GPI-anchor biosynthesis in the endoplasmic reticulum.
MedLine Citation:
PMID:  19815513     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Noriyuki Kanzawa; Yusuke Maeda; Hideo Ogiso; Yoshiko Murakami; Ryo Taguchi; Taroh Kinoshita
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2009-10-07
Journal Detail:
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:
Created Date:  2009-10-21     Completed Date:  2009-11-23     Revised Date:  2010-09-28    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  United States    
Other Details:
Languages:  eng     Pagination:  17711-6     Citation Subset:  IM    
Affiliation:
Research Institute for Microbial Diseases, Osaka University, Suita-city, Osaka 565-0871, Japan.
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MeSH Terms
Descriptor/Qualifier:
Acyltransferases / 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:
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

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