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Article: Plant cytosolic acyl-CoA-binding proteins

TitlePlant cytosolic acyl-CoA-binding proteins
Authors
KeywordsAcyl-CoA
Fluorescence
Gene expression
Lipid analysis
Lipid metabolism
Lipid trafficking
Issue Date2016
PublisherSpringer for AOCS Press. The Journal's web site is located at http://www.aocs.org/press/lipids.htm
Citation
Lipids, 2016, v. 51 n. 1, p. 1-13 How to Cite?
AbstractA gene family encoding six members of acyl-CoA-binding proteins (ACBP) exists in Arabidopsis and they are designated as AtACBP1-AtACBP6. They have been observed to play pivotal roles in plant lipid metabolism, consistent to the abilities of recombinant AtACBP in binding different medium- and long-chain acyl-CoA esters in vitro. While AtACBP1 and AtACBP2 are membrane-associated proteins with ankyrin repeats and AtACBP3 contains a signaling peptide for targeting to the apoplast, AtACBP4, AtACBP5 and AtACBP6 represent the cytosolic forms in the AtACBP family. They were verified to be subcellularly localized in the cytosol using diverse experimental methods, including cell fractionation followed by western blot analysis, immunoelectron microscopy and confocal laser-scanning microscopy using autofluorescence-tagged fusions. AtACBP4 (73.2 kDa) and AtACBP5 (70.1 kDa) are the largest, while AtACBP6 (10.4 kDa) is the smallest. Their binding affinities to oleoyl-CoA esters suggested that they can potentially transfer oleoyl-CoA esters from the plastids to the endoplasmic reticulum, facilitating the subsequent biosynthesis of non-plastidial membrane lipids in Arabidopsis. Recent studies on ACBP, extended from a dicot (Arabidopsis) to a monocot, revealed that six ACBP are also encoded in rice (Oryza sativa). Interestingly, three small rice ACBP (OsACBP1, OsACBP2 and OsACBP3) are present in the cytosol in comparison to one (AtACBP6) in Arabidopsis. In this review, the combinatory and distinct roles of the cytosolic AtACBP are discussed, including their functions in pollen and seed development, light-dependent regulation and substrate affinities to acyl-CoA esters.
Persistent Identifierhttp://hdl.handle.net/10722/230264
ISSN
2023 Impact Factor: 1.8
2023 SCImago Journal Rankings: 0.438
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorYe, Z-
dc.contributor.authorChye, ML-
dc.date.accessioned2016-08-23T14:16:03Z-
dc.date.available2016-08-23T14:16:03Z-
dc.date.issued2016-
dc.identifier.citationLipids, 2016, v. 51 n. 1, p. 1-13-
dc.identifier.issn0024-4201-
dc.identifier.urihttp://hdl.handle.net/10722/230264-
dc.description.abstractA gene family encoding six members of acyl-CoA-binding proteins (ACBP) exists in Arabidopsis and they are designated as AtACBP1-AtACBP6. They have been observed to play pivotal roles in plant lipid metabolism, consistent to the abilities of recombinant AtACBP in binding different medium- and long-chain acyl-CoA esters in vitro. While AtACBP1 and AtACBP2 are membrane-associated proteins with ankyrin repeats and AtACBP3 contains a signaling peptide for targeting to the apoplast, AtACBP4, AtACBP5 and AtACBP6 represent the cytosolic forms in the AtACBP family. They were verified to be subcellularly localized in the cytosol using diverse experimental methods, including cell fractionation followed by western blot analysis, immunoelectron microscopy and confocal laser-scanning microscopy using autofluorescence-tagged fusions. AtACBP4 (73.2 kDa) and AtACBP5 (70.1 kDa) are the largest, while AtACBP6 (10.4 kDa) is the smallest. Their binding affinities to oleoyl-CoA esters suggested that they can potentially transfer oleoyl-CoA esters from the plastids to the endoplasmic reticulum, facilitating the subsequent biosynthesis of non-plastidial membrane lipids in Arabidopsis. Recent studies on ACBP, extended from a dicot (Arabidopsis) to a monocot, revealed that six ACBP are also encoded in rice (Oryza sativa). Interestingly, three small rice ACBP (OsACBP1, OsACBP2 and OsACBP3) are present in the cytosol in comparison to one (AtACBP6) in Arabidopsis. In this review, the combinatory and distinct roles of the cytosolic AtACBP are discussed, including their functions in pollen and seed development, light-dependent regulation and substrate affinities to acyl-CoA esters.-
dc.languageeng-
dc.publisherSpringer for AOCS Press. The Journal's web site is located at http://www.aocs.org/press/lipids.htm-
dc.relation.ispartofLipids-
dc.rightsThe final publication is available at Springer via http://dx.doi.org/[insert DOI]-
dc.subjectAcyl-CoA-
dc.subjectFluorescence-
dc.subjectGene expression-
dc.subjectLipid analysis-
dc.subjectLipid metabolism-
dc.subjectLipid trafficking-
dc.titlePlant cytosolic acyl-CoA-binding proteins-
dc.typeArticle-
dc.identifier.emailChye, ML: mlchye@hkucc.hku.hk-
dc.identifier.authorityChye, ML=rp00687-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1007/s11745-015-4103-z-
dc.identifier.pmid26662549-
dc.identifier.scopuseid_2-s2.0-84952984572-
dc.identifier.hkuros260379-
dc.identifier.volume51-
dc.identifier.issue1-
dc.identifier.spage1-
dc.identifier.epage13-
dc.identifier.isiWOS:000367542400001-
dc.publisher.placeUnited States-
dc.identifier.issnl0024-4201-

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