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Article: The Arabidopsis thaliana ACBP3 regulates leaf senescence by modulating phospholipid metabolism and ATG8 stability

TitleThe Arabidopsis thaliana ACBP3 regulates leaf senescence by modulating phospholipid metabolism and ATG8 stability
Authors
Issue Date2010
Citation
Autophagy, 2010, v. 6 n. 6, p. 802-804 How to Cite?
AbstractBulk 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 Identifierhttp://hdl.handle.net/10722/179206
ISSN
2015 Impact Factor: 9.108
2015 SCImago Journal Rankings: 3.916

 

DC FieldValueLanguage
dc.contributor.authorXiao, Sen_US
dc.contributor.authorChye, MLen_US
dc.date.accessioned2012-12-19T09:52:55Z-
dc.date.available2012-12-19T09:52:55Z-
dc.date.issued2010en_US
dc.identifier.citationAutophagy, 2010, v. 6 n. 6, p. 802-804en_US
dc.identifier.issn1554-8627en_US
dc.identifier.urihttp://hdl.handle.net/10722/179206-
dc.description.abstractBulk 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.languageengen_US
dc.relation.ispartofAutophagyen_US
dc.subject.meshArabidopsis - Cytology - Metabolismen_US
dc.subject.meshArabidopsis Proteins - Metabolismen_US
dc.subject.meshAutophagyen_US
dc.subject.meshCarrier Proteins - Metabolismen_US
dc.subject.meshCell Agingen_US
dc.subject.meshModels, Biologicalen_US
dc.subject.meshPhagosomes - Metabolismen_US
dc.subject.meshPhospholipids - Metabolismen_US
dc.subject.meshPlant Leaves - Cytology - Metabolismen_US
dc.subject.meshProtein Stabilityen_US
dc.titleThe Arabidopsis thaliana ACBP3 regulates leaf senescence by modulating phospholipid metabolism and ATG8 stabilityen_US
dc.typeArticleen_US
dc.identifier.emailXiao, S: xiaoshi@graduate.hku.hken_US
dc.identifier.emailChye, ML: mlchye@hkucc.hku.hken_US
dc.identifier.authorityXiao, S=rp00817en_US
dc.identifier.authorityChye, ML=rp00687en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.4161/auto.6.6.12576en_US
dc.identifier.pmid20574160-
dc.identifier.scopuseid_2-s2.0-77955876036en_US
dc.identifier.hkuros179157-
dc.identifier.volume6en_US
dc.identifier.issue6en_US
dc.identifier.spage802en_US
dc.identifier.epage804en_US
dc.identifier.scopusauthoridXiao, S=7402022635en_US
dc.identifier.scopusauthoridChye, ML=7003905460en_US

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