Reassessing the Potential Activities of Plant CGI-58 Protein
Identifieur interne : 000064 ( Main/Exploration ); précédent : 000063; suivant : 000065Reassessing the Potential Activities of Plant CGI-58 Protein
Auteurs : Abdallah Khatib ; Yani Arhab ; Assia Bentebibel ; Abdelkarim Abousalham ; Alexandre NoirielSource :
- PLoS ONE [ 1932-6203 ] ; 2016.
Abstract
Comparative Gene Identification-58 (CGI-58) is a widespread protein found in animals and plants. This protein has been shown to participate in lipolysis in mice and humans by activating Adipose triglyceride lipase (ATGL), the initial enzyme responsible for the triacylglycerol (TAG) catabolism cascade. Human mutation of CGI-58 is the cause of Chanarin-Dorfman syndrome, an orphan disease characterized by a systemic accumulation of TAG which engenders tissue disorders. The CGI-58 protein has also been shown to participate in neutral lipid metabolism in plants and, in this case, a mutation again provokes TAG accumulation. Although its roles as an ATGL coactivator and in lipid metabolism are quite clear, the catalytic activity of CGI-58 is still in question. The acyltransferase activities of CGI-58 have been speculated about, reported or even dismissed and experimental evidence that CGI-58 expressed in
Url:
DOI: 10.1371/journal.pone.0145806
PubMed: 26745266
PubMed Central: 4706320
Affiliations:
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Reassessing the Potential Activities of Plant CGI-58 Protein</title><author><name sortKey="Khatib, Abdallah" sort="Khatib, Abdallah" uniqKey="Khatib A" first="Abdallah" last="Khatib">Abdallah Khatib</name><affiliation><nlm:aff id="aff001"></nlm:aff></affiliation></author><author><name sortKey="Arhab, Yani" sort="Arhab, Yani" uniqKey="Arhab Y" first="Yani" last="Arhab">Yani Arhab</name><affiliation><nlm:aff id="aff001"></nlm:aff></affiliation></author><author><name sortKey="Bentebibel, Assia" sort="Bentebibel, Assia" uniqKey="Bentebibel A" first="Assia" last="Bentebibel">Assia Bentebibel</name><affiliation><nlm:aff id="aff001"></nlm:aff></affiliation></author><author><name sortKey="Abousalham, Abdelkarim" sort="Abousalham, Abdelkarim" uniqKey="Abousalham A" first="Abdelkarim" last="Abousalham">Abdelkarim Abousalham</name><affiliation><nlm:aff id="aff001"></nlm:aff></affiliation></author><author><name sortKey="Noiriel, Alexandre" sort="Noiriel, Alexandre" uniqKey="Noiriel A" first="Alexandre" last="Noiriel">Alexandre Noiriel</name><affiliation><nlm:aff id="aff001"></nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">26745266</idno><idno type="pmc">4706320</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4706320</idno><idno type="RBID">PMC:4706320</idno><idno type="doi">10.1371/journal.pone.0145806</idno><date when="2016">2016</date><idno type="wicri:Area/Pmc/Corpus">000206</idno><idno type="wicri:Area/Pmc/Curation">000206</idno><idno type="wicri:Area/Pmc/Checkpoint">000049</idno><idno type="wicri:Area/Ncbi/Merge">001E53</idno><idno type="wicri:Area/Ncbi/Curation">001E53</idno><idno type="wicri:Area/Ncbi/Checkpoint">001E53</idno><idno type="wicri:Area/Main/Merge">000064</idno><idno type="wicri:Area/Main/Curation">000064</idno><idno type="wicri:Area/Main/Exploration">000064</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Reassessing the Potential Activities of Plant CGI-58 Protein</title><author><name sortKey="Khatib, Abdallah" sort="Khatib, Abdallah" uniqKey="Khatib A" first="Abdallah" last="Khatib">Abdallah Khatib</name><affiliation><nlm:aff id="aff001"></nlm:aff></affiliation></author><author><name sortKey="Arhab, Yani" sort="Arhab, Yani" uniqKey="Arhab Y" first="Yani" last="Arhab">Yani Arhab</name><affiliation><nlm:aff id="aff001"></nlm:aff></affiliation></author><author><name sortKey="Bentebibel, Assia" sort="Bentebibel, Assia" uniqKey="Bentebibel A" first="Assia" last="Bentebibel">Assia Bentebibel</name><affiliation><nlm:aff id="aff001"></nlm:aff></affiliation></author><author><name sortKey="Abousalham, Abdelkarim" sort="Abousalham, Abdelkarim" uniqKey="Abousalham A" first="Abdelkarim" last="Abousalham">Abdelkarim Abousalham</name><affiliation><nlm:aff id="aff001"></nlm:aff></affiliation></author><author><name sortKey="Noiriel, Alexandre" sort="Noiriel, Alexandre" uniqKey="Noiriel A" first="Alexandre" last="Noiriel">Alexandre Noiriel</name><affiliation><nlm:aff id="aff001"></nlm:aff></affiliation></author></analytic><series><title level="j">PLoS ONE</title><idno type="eISSN">1932-6203</idno><imprint><date when="2016">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Comparative Gene Identification-58 (CGI-58) is a widespread protein found in animals and plants. This protein has been shown to participate in lipolysis in mice and humans by activating Adipose triglyceride lipase (ATGL), the initial enzyme responsible for the triacylglycerol (TAG) catabolism cascade. Human mutation of CGI-58 is the cause of Chanarin-Dorfman syndrome, an orphan disease characterized by a systemic accumulation of TAG which engenders tissue disorders. The CGI-58 protein has also been shown to participate in neutral lipid metabolism in plants and, in this case, a mutation again provokes TAG accumulation. Although its roles as an ATGL coactivator and in lipid metabolism are quite clear, the catalytic activity of CGI-58 is still in question. The acyltransferase activities of CGI-58 have been speculated about, reported or even dismissed and experimental evidence that CGI-58 expressed in <italic>E</italic>. <italic>coli</italic> possesses an unambiguous catalytic activity is still lacking. To address this problem, we developed a new set of plasmids and site-directed mutants to elucidate the <italic>in vivo</italic> effects of CGI-58 expression on lipid metabolism in <italic>E</italic>. <italic>coli</italic>. By analyzing the lipid composition in selected <italic>E</italic>. <italic>coli</italic> strains expressing CGI-58 proteins, and by reinvestigating enzymatic tests with adequate controls, we show here that recombinant plant CGI-58 has none of the proposed activities previously described. Recombinant plant and mouse CGI-58 both lack acyltransferase activity towards either lysophosphatidylglycerol or lysophosphatidic acid to form phosphatidylglycerol or phosphatidic acid and recombinant plant CGI-58 does not catalyze TAG or phospholipid hydrolysis. However, expression of recombinant plant CGI-58, but not mouse CGI-58, led to a decrease in phosphatidylglycerol in all strains of <italic>E</italic>. <italic>coli</italic> tested, and a mutation of the putative catalytic residues restored a wild-type phenotype. 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Zechner</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Heath, Rj" uniqKey="Heath R">RJ Heath</name></author><author><name sortKey="Rock, Co" uniqKey="Rock C">CO Rock</name></author></analytic></biblStruct></listBibl></div1></back></TEI><affiliations><list></list><tree><noCountry><name sortKey="Abousalham, Abdelkarim" sort="Abousalham, Abdelkarim" uniqKey="Abousalham A" first="Abdelkarim" last="Abousalham">Abdelkarim Abousalham</name><name sortKey="Arhab, Yani" sort="Arhab, Yani" uniqKey="Arhab Y" first="Yani" last="Arhab">Yani Arhab</name><name sortKey="Bentebibel, Assia" sort="Bentebibel, Assia" uniqKey="Bentebibel A" first="Assia" last="Bentebibel">Assia Bentebibel</name><name sortKey="Khatib, Abdallah" sort="Khatib, Abdallah" uniqKey="Khatib A" first="Abdallah" last="Khatib">Abdallah Khatib</name><name sortKey="Noiriel, Alexandre" sort="Noiriel, Alexandre" uniqKey="Noiriel A" first="Alexandre" last="Noiriel">Alexandre 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