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- Publisher Website: 10.1016/j.plipres.2010.11.002
- Scopus: eid_2-s2.0-78651260650
- PMID: 21144863
- WOS: WOS:000289543800002
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Article: New roles for acyl-CoA-binding proteins (ACBPs) in plant development, stress responses and lipid metabolism
Title | New roles for acyl-CoA-binding proteins (ACBPs) in plant development, stress responses and lipid metabolism | ||||||||
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Authors | |||||||||
Keywords | Acyl-CoA-binding domain Embryogenesis Freezing tolerance Heavy metal resistance Leaf senescence Oxidative stress Phospholipid metabolism | ||||||||
Issue Date | 2011 | ||||||||
Publisher | Pergamon. 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? | ||||||||
Abstract | ACBPs 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 Identifier | http://hdl.handle.net/10722/133736 | ||||||||
ISSN | 2023 Impact Factor: 14.0 2023 SCImago Journal Rankings: 3.638 | ||||||||
ISI Accession Number ID |
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 Field | Value | Language |
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dc.contributor.author | Xiao, S | en_HK |
dc.contributor.author | Chye, ML | en_HK |
dc.date.accessioned | 2011-05-24T02:17:17Z | - |
dc.date.available | 2011-05-24T02:17:17Z | - |
dc.date.issued | 2011 | en_HK |
dc.identifier.citation | Progress In Lipid Research, 2011, v. 50 n. 2, p. 141-151 | en_HK |
dc.identifier.issn | 0163-7827 | en_HK |
dc.identifier.uri | http://hdl.handle.net/10722/133736 | - |
dc.description.abstract | ACBPs 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.language | eng | en_US |
dc.publisher | Pergamon. The Journal's web site is located at http://www.elsevier.com/locate/plipres | en_HK |
dc.relation.ispartof | Progress in Lipid Research | en_HK |
dc.rights | Appropriate 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.subject | Acyl-CoA-binding domain | en_HK |
dc.subject | Embryogenesis | en_HK |
dc.subject | Freezing tolerance | en_HK |
dc.subject | Heavy metal resistance | en_HK |
dc.subject | Leaf senescence | en_HK |
dc.subject | Oxidative stress | en_HK |
dc.subject | Phospholipid metabolism | en_HK |
dc.title | New roles for acyl-CoA-binding proteins (ACBPs) in plant development, stress responses and lipid metabolism | en_HK |
dc.type | Article | en_HK |
dc.identifier.openurl | http://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.email | Xiao, S: xiaoshi@graduate.hku.hk | en_HK |
dc.identifier.email | Chye, ML: mlchye@hkucc.hku.hk | en_HK |
dc.identifier.authority | Xiao, S=rp00817 | en_HK |
dc.identifier.authority | Chye, ML=rp00687 | en_HK |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1016/j.plipres.2010.11.002 | en_HK |
dc.identifier.pmid | 21144863 | - |
dc.identifier.scopus | eid_2-s2.0-78651260650 | en_HK |
dc.identifier.hkuros | 185388 | en_US |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-78651260650&selection=ref&src=s&origin=recordpage | en_HK |
dc.identifier.volume | 50 | en_HK |
dc.identifier.issue | 2 | en_HK |
dc.identifier.spage | 141 | en_HK |
dc.identifier.epage | 151 | en_HK |
dc.identifier.isi | WOS:000289543800002 | - |
dc.publisher.place | United Kingdom | en_HK |
dc.identifier.scopusauthorid | Xiao, S=7402022635 | en_HK |
dc.identifier.scopusauthorid | Chye, ML=7003905460 | en_HK |
dc.identifier.citeulike | 8411761 | - |
dc.identifier.issnl | 0163-7827 | - |