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- Publisher Website: 10.1016/j.bbalip.2015.12.018
- Scopus: eid_2-s2.0-84970002329
- PMID: 26747650
- WOS: WOS:000381533900019
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Article: The binding versatility of plant acyl-CoA-binding proteins and their significance in lipid metabolism
Title | The binding versatility of plant acyl-CoA-binding proteins and their significance in lipid metabolism |
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Authors | |
Keywords | Ankyrin repeat Fatty acid Heavy metal Interactor Kelch motif Phospholipid |
Issue Date | 2016 |
Publisher | Elsevier 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? |
Abstract | Acyl-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. |
Description | Special Issue on Plant lipid biology |
Persistent Identifier | http://hdl.handle.net/10722/234258 |
ISSN | 2023 Impact Factor: 3.9 2023 SCImago Journal Rankings: 1.365 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Lung, SC | - |
dc.contributor.author | Chye, ML | - |
dc.date.accessioned | 2016-10-14T07:00:10Z | - |
dc.date.available | 2016-10-14T07:00:10Z | - |
dc.date.issued | 2016 | - |
dc.identifier.citation | Biochimica et Biophysica Acta: Molecular and Cell Biology of Lipids, 2016, v. 1861 n. 9, pt. B, p. 1409-1421 | - |
dc.identifier.issn | 1388-1981 | - |
dc.identifier.uri | http://hdl.handle.net/10722/234258 | - |
dc.description | Special Issue on Plant lipid biology | - |
dc.description.abstract | Acyl-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.language | eng | - |
dc.publisher | Elsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/issn/13881981 | - |
dc.relation.ispartof | Biochimica et Biophysica Acta: Molecular and Cell Biology of Lipids | - |
dc.subject | Ankyrin repeat | - |
dc.subject | Fatty acid | - |
dc.subject | Heavy metal | - |
dc.subject | Interactor | - |
dc.subject | Kelch motif | - |
dc.subject | Phospholipid | - |
dc.title | The binding versatility of plant acyl-CoA-binding proteins and their significance in lipid metabolism | - |
dc.type | Article | - |
dc.identifier.email | Lung, SC: sclung@hku.hk | - |
dc.identifier.email | Chye, ML: mlchye@hkucc.hku.hk | - |
dc.identifier.authority | Chye, ML=rp00687 | - |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1016/j.bbalip.2015.12.018 | - |
dc.identifier.pmid | 26747650 | - |
dc.identifier.scopus | eid_2-s2.0-84970002329 | - |
dc.identifier.hkuros | 267758 | - |
dc.identifier.volume | 1861 | - |
dc.identifier.issue | 9, pt. B | - |
dc.identifier.spage | 1409 | - |
dc.identifier.epage | 1421 | - |
dc.identifier.isi | WOS:000381533900019 | - |
dc.publisher.place | Netherlands | - |
dc.identifier.issnl | 1388-1981 | - |