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Article: The binding versatility of plant acyl-CoA-binding proteins and their significance in lipid metabolism

TitleThe binding versatility of plant acyl-CoA-binding proteins and their significance in lipid metabolism
Authors
KeywordsAnkyrin repeat
Fatty acid
Heavy metal
Interactor
Kelch motif
Phospholipid
Issue Date2016
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/issn/13881981
Citation
Biochimica et Biophysica Acta: Molecular and Cell Biology of Lipids, 2016, v. 1861 n. 9, pt. B, p. 1409-1421 How to Cite?
AbstractAcyl-CoA esters are the activated form of fatty acids and play important roles in lipid metabolism and the regulation of cell functions. They are bound and transported by nonenzymic proteins such as the acyl-CoA-binding proteins (ACBPs). Although plant ACBPs were so named by virtue of amino acid homology to existing yeast and mammalian counterparts, recent studies revealed that ligand specificities of plant ACBPs are not restricted to acyl-CoA esters. Arabidopsis and rice ACBPs also interact with phospholipids, and their affinities to different acyl-CoA species and phospholipid classes vary amongst isoforms. Their ligands also include heavy metals. Interactors of plant ACBPs are further diversified due to the evolution of protein–protein interacting domains. This review summarizes our current understanding of plant ACBPs with a focus on their binding versatility. Their broad ligand range is of paramount significance in serving a multitude of functions during development and stress responses as discussed herein. This article is part of a Special Issue entitled: Plant Lipid Biology edited by Kent D. Chapman and Ivo Feussner.
DescriptionSpecial Issue on Plant lipid biology
Persistent Identifierhttp://hdl.handle.net/10722/234258
ISSN
2021 Impact Factor: 5.228
2020 SCImago Journal Rankings: 1.769
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorLung, SC-
dc.contributor.authorChye, ML-
dc.date.accessioned2016-10-14T07:00:10Z-
dc.date.available2016-10-14T07:00:10Z-
dc.date.issued2016-
dc.identifier.citationBiochimica et Biophysica Acta: Molecular and Cell Biology of Lipids, 2016, v. 1861 n. 9, pt. B, p. 1409-1421-
dc.identifier.issn1388-1981-
dc.identifier.urihttp://hdl.handle.net/10722/234258-
dc.descriptionSpecial Issue on Plant lipid biology-
dc.description.abstractAcyl-CoA esters are the activated form of fatty acids and play important roles in lipid metabolism and the regulation of cell functions. They are bound and transported by nonenzymic proteins such as the acyl-CoA-binding proteins (ACBPs). Although plant ACBPs were so named by virtue of amino acid homology to existing yeast and mammalian counterparts, recent studies revealed that ligand specificities of plant ACBPs are not restricted to acyl-CoA esters. Arabidopsis and rice ACBPs also interact with phospholipids, and their affinities to different acyl-CoA species and phospholipid classes vary amongst isoforms. Their ligands also include heavy metals. Interactors of plant ACBPs are further diversified due to the evolution of protein–protein interacting domains. This review summarizes our current understanding of plant ACBPs with a focus on their binding versatility. Their broad ligand range is of paramount significance in serving a multitude of functions during development and stress responses as discussed herein. This article is part of a Special Issue entitled: Plant Lipid Biology edited by Kent D. Chapman and Ivo Feussner.-
dc.languageeng-
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/issn/13881981-
dc.relation.ispartofBiochimica et Biophysica Acta: Molecular and Cell Biology of Lipids-
dc.subjectAnkyrin repeat-
dc.subjectFatty acid-
dc.subjectHeavy metal-
dc.subjectInteractor-
dc.subjectKelch motif-
dc.subjectPhospholipid-
dc.titleThe binding versatility of plant acyl-CoA-binding proteins and their significance in lipid metabolism-
dc.typeArticle-
dc.identifier.emailLung, SC: sclung@hku.hk-
dc.identifier.emailChye, ML: mlchye@hkucc.hku.hk-
dc.identifier.authorityChye, ML=rp00687-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.bbalip.2015.12.018-
dc.identifier.pmid26747650-
dc.identifier.scopuseid_2-s2.0-84970002329-
dc.identifier.hkuros267758-
dc.identifier.volume1861-
dc.identifier.issue9, pt. B-
dc.identifier.spage1409-
dc.identifier.epage1421-
dc.identifier.isiWOS:000381533900019-
dc.publisher.placeNetherlands-
dc.identifier.issnl1388-1981-

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