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- Publisher Website: 10.4161/auto.6.6.12576
- Scopus: eid_2-s2.0-77955876036
- PMID: 20574160
- WOS: WOS:000280971000014
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Article: The Arabidopsis thaliana ACBP3 regulates leaf senescence by modulating phospholipid metabolism and ATG8 stability
Title | The Arabidopsis thaliana ACBP3 regulates leaf senescence by modulating phospholipid metabolism and ATG8 stability |
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Authors | |
Keywords | Acyl-CoA-binding proteins ATG8 Autophagosome formation Leaf senescence Phosphatidylethanolamine metabolism Phospholipid binding |
Issue Date | 2010 |
Citation | Autophagy, 2010, v. 6 n. 6, p. 802-804 How to Cite? |
Abstract | Bulk degradation and nutrient recycling are events associated with autophagy. The core components of the autophagy machinery have been elucidated recently using molecular and genetic approaches. In particular, two ubiquitin-like proteins, ATG8 and ATG12, which conjugate with phosphatidylethanolamine (PE) and ATG5, respectively, forming ATG8-PE and ATG12-ATG5 complexes, were shown to be essential in autophagosome formation. Our recent findings reveal that the Arabidopsis thaliana acyl-CoA-binding protein ACBP3 binds the phospholipid PE in vitro and that ACBP3 overexpression and downregulation correlate with PE composition in rosettes. Furthermore, ACBP3-overexpressors (ACBP3-OEs) display accelerated salicylic acid-dependent leaf senescence resembling the phenotype of Arabidopsis knockout (KO) mutants defective in autophagy-related (ATG) proteins. Consistently, downregulation of ACBP3 (ACBP3-KOs) delays dark-induced leaf senescence. By analysis of transgenic Arabidopsis expressing GFP-ATG8e as well as those co-expressing ACBP3-OE and GFP-ATG8e, we showed that ACBP3-overexpression disrupts autophagosome formation and enhanced degradation of ATG8 under starvation conditions, suggesting that ACBP3 is an important regulator of the ATG8-PE complex via its interaction with PE. Here, a working model for the role of ACBP3 in the regulation of autophagy-mediated leaf senescence is presented. © 2010 Landes Bioscience. |
Persistent Identifier | http://hdl.handle.net/10722/179206 |
ISSN | 2023 Impact Factor: 14.6 2023 SCImago Journal Rankings: 4.035 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Xiao, S | en_US |
dc.contributor.author | Chye, ML | en_US |
dc.date.accessioned | 2012-12-19T09:52:55Z | - |
dc.date.available | 2012-12-19T09:52:55Z | - |
dc.date.issued | 2010 | en_US |
dc.identifier.citation | Autophagy, 2010, v. 6 n. 6, p. 802-804 | en_US |
dc.identifier.issn | 1554-8627 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/179206 | - |
dc.description.abstract | Bulk degradation and nutrient recycling are events associated with autophagy. The core components of the autophagy machinery have been elucidated recently using molecular and genetic approaches. In particular, two ubiquitin-like proteins, ATG8 and ATG12, which conjugate with phosphatidylethanolamine (PE) and ATG5, respectively, forming ATG8-PE and ATG12-ATG5 complexes, were shown to be essential in autophagosome formation. Our recent findings reveal that the Arabidopsis thaliana acyl-CoA-binding protein ACBP3 binds the phospholipid PE in vitro and that ACBP3 overexpression and downregulation correlate with PE composition in rosettes. Furthermore, ACBP3-overexpressors (ACBP3-OEs) display accelerated salicylic acid-dependent leaf senescence resembling the phenotype of Arabidopsis knockout (KO) mutants defective in autophagy-related (ATG) proteins. Consistently, downregulation of ACBP3 (ACBP3-KOs) delays dark-induced leaf senescence. By analysis of transgenic Arabidopsis expressing GFP-ATG8e as well as those co-expressing ACBP3-OE and GFP-ATG8e, we showed that ACBP3-overexpression disrupts autophagosome formation and enhanced degradation of ATG8 under starvation conditions, suggesting that ACBP3 is an important regulator of the ATG8-PE complex via its interaction with PE. Here, a working model for the role of ACBP3 in the regulation of autophagy-mediated leaf senescence is presented. © 2010 Landes Bioscience. | en_US |
dc.language | eng | en_US |
dc.relation.ispartof | Autophagy | en_US |
dc.subject | Acyl-CoA-binding proteins | - |
dc.subject | ATG8 | - |
dc.subject | Autophagosome formation | - |
dc.subject | Leaf senescence | - |
dc.subject | Phosphatidylethanolamine metabolism | - |
dc.subject | Phospholipid binding | - |
dc.subject.mesh | Arabidopsis - Cytology - Metabolism | en_US |
dc.subject.mesh | Arabidopsis Proteins - Metabolism | en_US |
dc.subject.mesh | Autophagy | en_US |
dc.subject.mesh | Carrier Proteins - Metabolism | en_US |
dc.subject.mesh | Cell Aging | en_US |
dc.subject.mesh | Models, Biological | en_US |
dc.subject.mesh | Phagosomes - Metabolism | en_US |
dc.subject.mesh | Phospholipids - Metabolism | en_US |
dc.subject.mesh | Plant Leaves - Cytology - Metabolism | en_US |
dc.subject.mesh | Protein Stability | en_US |
dc.title | The Arabidopsis thaliana ACBP3 regulates leaf senescence by modulating phospholipid metabolism and ATG8 stability | en_US |
dc.type | Article | en_US |
dc.identifier.email | Xiao, S: xiaoshi@graduate.hku.hk | en_US |
dc.identifier.email | Chye, ML: mlchye@hkucc.hku.hk | en_US |
dc.identifier.authority | Xiao, S=rp00817 | en_US |
dc.identifier.authority | Chye, ML=rp00687 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.doi | 10.4161/auto.6.6.12576 | en_US |
dc.identifier.pmid | 20574160 | - |
dc.identifier.scopus | eid_2-s2.0-77955876036 | en_US |
dc.identifier.hkuros | 179157 | - |
dc.identifier.volume | 6 | en_US |
dc.identifier.issue | 6 | en_US |
dc.identifier.spage | 802 | en_US |
dc.identifier.epage | 804 | en_US |
dc.identifier.isi | WOS:000280971000014 | - |
dc.identifier.scopusauthorid | Xiao, S=7402022635 | en_US |
dc.identifier.scopusauthorid | Chye, ML=7003905460 | en_US |
dc.identifier.issnl | 1554-8627 | - |