| http://purl.uniprot.org/citations/24879803 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/24879803 | http://www.w3.org/2000/01/rdf-schema#comment | "Mutations in the gene encoding comparative gene identification 58 (CGI-58)/α/β hydrolase domain 5 (ABHD5) cause Chanarin-Dorfman syndrome, characterized by excessive triacylglycerol storage in cells and tissues. CGI-58 has been identified as a coactivator of adipose TG lipase (ATGL) and a lysophosphatidic acid acyltransferase (LPAAT). We developed a molecular model of CGI-58 structure and then mutated predicted active site residues and performed LPAAT activity assays of recombinant WT and mutated CGI-58. When mutations of predicted catalytic residues failed to reduce LPAAT activity, we determined that LPAAT activity was due to a bacterial contaminant of affinity purification procedures, plsC, the sole LPAAT in Escherichia coli Purification protocols were optimized to reduce plsC contamination, in turn reducing LPAAT activity. When CGI-58 was expressed in SM2-1(DE3) cells that lack plsC, lysates lacked LPAAT activity. Additionally, mouse CGI-58 expressed in bacteria as a glutathione-S-transferase fusion protein and human CGI-58 expressed in yeast lacked LPAAT activity. Previously reported lipid binding activity of CGI-58 was revisited using protein-lipid overlays. Recombinant CGI-58 failed to bind lysophosphatidic acid, but interestingly, bound phosphatidylinositol 3-phosphate [PI(3)P] and phosphatidylinositol 5-phosphate [PI(5)P]. Prebinding CGI-58 with PI(3)P or PI(5)P did not alter its coactivation of ATGL in vitro. In summary, purified recombinant CGI-58 that is functional as an ATGL coactivator lacks LPAAT activity."xsd:string |
| http://purl.uniprot.org/citations/24879803 | http://purl.org/dc/terms/identifier | "doi:10.1194/jlr.m051151"xsd:string |
| http://purl.uniprot.org/citations/24879803 | http://purl.uniprot.org/core/author | "Brasaemle D.L."xsd:string |
| http://purl.uniprot.org/citations/24879803 | http://purl.uniprot.org/core/author | "Carman G.M."xsd:string |
| http://purl.uniprot.org/citations/24879803 | http://purl.uniprot.org/core/author | "McMahon D."xsd:string |
| http://purl.uniprot.org/citations/24879803 | http://purl.uniprot.org/core/author | "Han G.S."xsd:string |
| http://purl.uniprot.org/citations/24879803 | http://purl.uniprot.org/core/author | "Shah D."xsd:string |
| http://purl.uniprot.org/citations/24879803 | http://purl.uniprot.org/core/author | "Kurz D."xsd:string |
| http://purl.uniprot.org/citations/24879803 | http://purl.uniprot.org/core/author | "Dinh A."xsd:string |
| http://purl.uniprot.org/citations/24879803 | http://purl.uniprot.org/core/date | "2014"xsd:gYear |
| http://purl.uniprot.org/citations/24879803 | http://purl.uniprot.org/core/name | "J Lipid Res"xsd:string |
| http://purl.uniprot.org/citations/24879803 | http://purl.uniprot.org/core/pages | "1750-1761"xsd:string |
| http://purl.uniprot.org/citations/24879803 | http://purl.uniprot.org/core/title | "Comparative gene identification 58/alpha/beta hydrolase domain 5 lacks lysophosphatidic acid acyltransferase activity."xsd:string |
| http://purl.uniprot.org/citations/24879803 | http://purl.uniprot.org/core/volume | "55"xsd:string |
| http://purl.uniprot.org/citations/24879803 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/24879803 |
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| http://purl.uniprot.org/uniprot/#_F6K7K3-mappedCitation-24879803 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/24879803 |
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| http://purl.uniprot.org/uniprot/#_A0A6B9MC78-mappedCitation-24879803 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/24879803 |