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Article: New roles for acyl-CoA-binding proteins (ACBPs) in plant development, stress responses and lipid metabolism

TitleNew roles for acyl-CoA-binding proteins (ACBPs) in plant development, stress responses and lipid metabolism
Authors
KeywordsAcyl-CoA-binding domain
Embryogenesis
Freezing tolerance
Heavy metal resistance
Leaf senescence
Oxidative stress
Phospholipid metabolism
Issue Date2011
PublisherPergamon. The Journal's web site is located at http://www.elsevier.com/locate/plipres
Citation
Progress In Lipid Research, 2011, v. 50 n. 2, p. 141-151 How to Cite?
AbstractACBPs are implicated in acyl-CoA trafficking in many eukaryotes and some prokaryotes. Six genes encode proteins designated as AtACBP1-AtACBP6 in the Arabidopsis thaliana ACBP family. These ACBPs are conserved in the acyl-CoA-binding domain, but vary in size from 92 amino acids (10.4 kDa) to 668 amino acids (73.1 kDa), and are subcellularly localised to different compartments in plant cells. Results from in vitro binding assays show that their corresponding recombinant proteins exhibit differential binding affinities to acyl-CoA esters and phospholipids, implying that these ACBPs may have non-redundant biological functions in vivo. By using knockout/downregulated and overexpression lines of Arabidopsis ACBPs, recent investigations have revealed that in addition to their proposed roles in phospholipid metabolism, these ACBPs can influence plant development including early embryogenesis and leaf senescence, as well as plant stress responses including heavy metal resistance, oxidative stress, freezing tolerance and pathogen resistance. In this review, recent progress on the biochemical and functional analyses of Arabidopsis ACBPs, their links to metabolic/signalling pathways, and their potential applications in development of stress tolerance are discussed. © 2010 Elsevier Ltd. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/133736
ISSN
2015 Impact Factor: 11.238
2015 SCImago Journal Rankings: 5.108
ISI Accession Number ID
Funding AgencyGrant Number
University of Hong Kong10208034
Research Grants Council of the Hong Kong Special Administrative Region, ChinaHKU7047/07M
University Grants Committee of the Hong Kong Special Administrative Region, ChinaAoE/B-07/99
Funding Information:

We thank the University of Hong Kong (Project 10208034 and postdoctoral fellowship to SX), the Research Grants Council of the Hong Kong Special Administrative Region, China (project HKU7047/07M) and the University Grants Committee of the Hong Kong Special Administrative Region, China (Project No. AoE/B-07/99) for support.

References

 

DC FieldValueLanguage
dc.contributor.authorXiao, Sen_HK
dc.contributor.authorChye, MLen_HK
dc.date.accessioned2011-05-24T02:17:17Z-
dc.date.available2011-05-24T02:17:17Z-
dc.date.issued2011en_HK
dc.identifier.citationProgress In Lipid Research, 2011, v. 50 n. 2, p. 141-151en_HK
dc.identifier.issn0163-7827en_HK
dc.identifier.urihttp://hdl.handle.net/10722/133736-
dc.description.abstractACBPs are implicated in acyl-CoA trafficking in many eukaryotes and some prokaryotes. Six genes encode proteins designated as AtACBP1-AtACBP6 in the Arabidopsis thaliana ACBP family. These ACBPs are conserved in the acyl-CoA-binding domain, but vary in size from 92 amino acids (10.4 kDa) to 668 amino acids (73.1 kDa), and are subcellularly localised to different compartments in plant cells. Results from in vitro binding assays show that their corresponding recombinant proteins exhibit differential binding affinities to acyl-CoA esters and phospholipids, implying that these ACBPs may have non-redundant biological functions in vivo. By using knockout/downregulated and overexpression lines of Arabidopsis ACBPs, recent investigations have revealed that in addition to their proposed roles in phospholipid metabolism, these ACBPs can influence plant development including early embryogenesis and leaf senescence, as well as plant stress responses including heavy metal resistance, oxidative stress, freezing tolerance and pathogen resistance. In this review, recent progress on the biochemical and functional analyses of Arabidopsis ACBPs, their links to metabolic/signalling pathways, and their potential applications in development of stress tolerance are discussed. © 2010 Elsevier Ltd. All rights reserved.en_HK
dc.languageengen_US
dc.publisherPergamon. The Journal's web site is located at http://www.elsevier.com/locate/plipresen_HK
dc.relation.ispartofProgress in Lipid Researchen_HK
dc.rightsAppropriate Bibliographic Citation:Authors posting Accepted Author Manuscript online should later add a citation for the Published Journal Article indicating that the Article was subsequently published, and may mention the journal title provided that they add the following text at the beginning of the document: “NOTICE: this is the author’s version of a work that was accepted for publication in <Journal title>. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in PUBLICATION, [VOL#, ISSUE#, (DATE)] DOI#”-
dc.subjectAcyl-CoA-binding domainen_HK
dc.subjectEmbryogenesisen_HK
dc.subjectFreezing toleranceen_HK
dc.subjectHeavy metal resistanceen_HK
dc.subjectLeaf senescenceen_HK
dc.subjectOxidative stressen_HK
dc.subjectPhospholipid metabolismen_HK
dc.titleNew roles for acyl-CoA-binding proteins (ACBPs) in plant development, stress responses and lipid metabolismen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0163-7827&volume=50&issue=2&spage=141&epage=151&date=2011&atitle=New+roles+for+acyl-CoA-binding+proteins+(ACBPS)+in+plant+development,+stress+responses+and+lipid+metabolism-
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.plipres.2010.11.002en_HK
dc.identifier.pmid21144863-
dc.identifier.scopuseid_2-s2.0-78651260650en_HK
dc.identifier.hkuros185388en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-78651260650&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume50en_HK
dc.identifier.issue2en_HK
dc.identifier.spage141en_HK
dc.identifier.epage151en_HK
dc.identifier.isiWOS:000289543800002-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridXiao, S=7402022635en_HK
dc.identifier.scopusauthoridChye, ML=7003905460en_HK
dc.identifier.citeulike8411761-

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