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Article: An Arabidopsis family of six acyl-CoA-binding proteins has three cytosolic members

TitleAn Arabidopsis family of six acyl-CoA-binding proteins has three cytosolic members
Authors
KeywordsAcyl-coenzyme A-binding protein
Arabidopsis thaliana
Cytosolic localization
Lipid trafficking
Oleoyl-CoA
Phospholipid binding
Issue Date2009
PublisherElsevier France, Editions Scientifiques et Medicales. The Journal's web site is located at http://www.elsevier.com/locate/plaphy
Citation
Plant Physiology And Biochemistry, 2009, v. 47 n. 6, p. 479-484 How to Cite?
AbstractIn Arabidopsis thaliana, a gene family of six members encodes acyl-CoA-binding proteins (ACBPs). These Arabidopsis ACBPs (designated ACBP1 to ACBP6) range in size from 10.4 kDa to 73.1 kDa and display varying affinities for acyl-CoA esters, suggesting that they have different roles in plant lipid metabolism. In contrast, only the 10-kDa ACBPs have been well-characterized from other eukaryote species. Our previous studies have revealed that ACBP1 and ACBP2 are membrane-associated proteins, while ACBP3 is extracellularly-targeted. More recently, we have reported that the remaining three members in this protein family (namely ACBP4, ACBP5 and ACBP6) are subcellularly localized to the cytosol in Arabidopsis. The subcellular localizations of ACBP4, ACBP5 and ACBP6 in the cytosol were demonstrated using a number of different approaches incorporating biochemical fractionation, confocal microscopy of transgenic Arabidopsis expressing autofluorescence-tagged fusions and immunoelectron microscopy using ACBP-specific antibodies. Our results indicate that all three ACBPs in the cytosol are potential candidates for acyl-CoA binding and trafficking in plant cells. In this review, the functional redundancy and differences among the three cytosolic ACBPs are discussed by comparison of their light-regulated expression and substrate affinities to acyl-CoA esters, and from biochemical analyses on their knockout mutants and/or overexpression in transgenic Arabidopsis. The transcriptionally light-induced ACBP4 and ACBP5, which encode the two largest forms of Arabidopsis ACBPs, bind oleoyl-CoA esters and likely transfer oleoyl-CoAs from the plastids (the site of de novo fatty acid biosynthesis) to the endoplasmic reticulum for the biosynthesis of non-plastidial membrane lipids in Arabidopsis. © 2008 Elsevier Masson SAS. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/60714
ISSN
2015 Impact Factor: 2.928
2015 SCImago Journal Rankings: 1.167
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorXiao, Sen_HK
dc.contributor.authorChye, MLen_HK
dc.date.accessioned2010-05-31T04:17:01Z-
dc.date.available2010-05-31T04:17:01Z-
dc.date.issued2009en_HK
dc.identifier.citationPlant Physiology And Biochemistry, 2009, v. 47 n. 6, p. 479-484en_HK
dc.identifier.issn0981-9428en_HK
dc.identifier.urihttp://hdl.handle.net/10722/60714-
dc.description.abstractIn Arabidopsis thaliana, a gene family of six members encodes acyl-CoA-binding proteins (ACBPs). These Arabidopsis ACBPs (designated ACBP1 to ACBP6) range in size from 10.4 kDa to 73.1 kDa and display varying affinities for acyl-CoA esters, suggesting that they have different roles in plant lipid metabolism. In contrast, only the 10-kDa ACBPs have been well-characterized from other eukaryote species. Our previous studies have revealed that ACBP1 and ACBP2 are membrane-associated proteins, while ACBP3 is extracellularly-targeted. More recently, we have reported that the remaining three members in this protein family (namely ACBP4, ACBP5 and ACBP6) are subcellularly localized to the cytosol in Arabidopsis. The subcellular localizations of ACBP4, ACBP5 and ACBP6 in the cytosol were demonstrated using a number of different approaches incorporating biochemical fractionation, confocal microscopy of transgenic Arabidopsis expressing autofluorescence-tagged fusions and immunoelectron microscopy using ACBP-specific antibodies. Our results indicate that all three ACBPs in the cytosol are potential candidates for acyl-CoA binding and trafficking in plant cells. In this review, the functional redundancy and differences among the three cytosolic ACBPs are discussed by comparison of their light-regulated expression and substrate affinities to acyl-CoA esters, and from biochemical analyses on their knockout mutants and/or overexpression in transgenic Arabidopsis. The transcriptionally light-induced ACBP4 and ACBP5, which encode the two largest forms of Arabidopsis ACBPs, bind oleoyl-CoA esters and likely transfer oleoyl-CoAs from the plastids (the site of de novo fatty acid biosynthesis) to the endoplasmic reticulum for the biosynthesis of non-plastidial membrane lipids in Arabidopsis. © 2008 Elsevier Masson SAS. All rights reserved.en_HK
dc.languageengen_HK
dc.publisherElsevier France, Editions Scientifiques et Medicales. The Journal's web site is located at http://www.elsevier.com/locate/plaphyen_HK
dc.relation.ispartofPlant Physiology and Biochemistryen_HK
dc.rightsPlant Physiology and Biochemistry. Copyright © Elsevier France, Editions Scientifiques et Medicales.en_HK
dc.subjectAcyl-coenzyme A-binding proteinen_HK
dc.subjectArabidopsis thalianaen_HK
dc.subjectCytosolic localizationen_HK
dc.subjectLipid traffickingen_HK
dc.subjectOleoyl-CoAen_HK
dc.subjectPhospholipid bindingen_HK
dc.titleAn Arabidopsis family of six acyl-CoA-binding proteins has three cytosolic membersen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0981-9428&volume=47&spage=479&epage=484&date=2009&atitle=An+Arabidopsis+family+of+six+acyl-CoA-binding+proteins+has+three+cytosolic+membersen_HK
dc.identifier.emailXiao, S: xiaoshi@graduate.hku.hken_HK
dc.identifier.emailChye, ML: mlchye@hkucc.hku.hken_HK
dc.identifier.authorityXiao, S=rp00817en_HK
dc.identifier.authorityChye, ML=rp00687en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.plaphy.2008.12.002en_HK
dc.identifier.pmid19121948-
dc.identifier.scopuseid_2-s2.0-64749102753en_HK
dc.identifier.hkuros157373en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-64749102753&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume47en_HK
dc.identifier.issue6en_HK
dc.identifier.spage479en_HK
dc.identifier.epage484en_HK
dc.identifier.isiWOS:000266272900007-
dc.publisher.placeFranceen_HK
dc.identifier.scopusauthoridXiao, S=7402022635en_HK
dc.identifier.scopusauthoridChye, ML=7003905460en_HK

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