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Article: Overexpression of Arabidopsis acyl-CoA binding protein ACBP3 promotes starvation-induced and age-dependent leaf senescence
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TitleOverexpression of Arabidopsis acyl-CoA binding protein ACBP3 promotes starvation-induced and age-dependent leaf senescence
 
AuthorsXiao, S2
Gao, W2
Chen, QF2
Chan, SW2
Zheng, SX2
Ma, J2
Wang, M2
Welti, R1
Chye, ML2
 
KeywordsBiology - botany
Biology - biochemistry
 
Issue Date2010
 
PublisherAmerican Society of Plant Biologists. The Journal's web site is located at http://www.plantcell.org
 
CitationPlant Cell, 2010, v. 22 n. 5, p. 1463-1482 [How to Cite?]
DOI: http://dx.doi.org/10.1105/tpc.110.075333
 
AbstractIn Arabidopsis thaliana, a family of six genes (ACBP1 to ACBP6) encodes acyl-CoA binding proteins (ACBPs). Investigations on ACBP3 reported here show its upregulation upon dark treatment and in senescing rosettes. Transgenic Arabidopsis overexpressing ACBP3 (ACBP3-OEs) displayed accelerated leaf senescence, whereas an acbp3 T-DNA insertional mutant and ACBP3 RNA interference transgenic Arabidopsis lines were delayed in dark-induced leaf senescence. Acyl-CoA and lipid profiling revealed that the overexpression of ACBP3 led to an increase in acyl-CoA and phosphatidylethanolamine (PE) levels, whereas ACBP3 downregulation reduced PE content. Moreover, significant losses in phosphatidylcholine (PC) and phosphatidylinositol, and gains in phosphatidic acid (PA), lysophospholipids, and oxylipin-containing galactolipids (arabidopsides) were evident in 3-week-old dark-treated and 6-week-old premature senescing ACBP3-OEs. Such accu-mulation of PA and arabidopsides (A, B, D, E, and G) resulting from lipid peroxidation in ACBP3-OEs likely promoted leaf senescence. The N-terminal signal sequence/transmembrane domain in ACBP3 was shown to be essential in ACBP3-green fluorescent protein targeting and in promoting senescence. Observations that recombinant ACBP3 binds PC, PE, and unsaturated acyl-CoAs in vitro and that ACBP3 overexpression enhances degradation of the autophagy (ATG)-related protein ATG8 and disrupts autophagosome formation suggest a role for ACBP3 as a phospholipid binding protein involved in the regulation of leaf senescence by modulating membrane phospholipid metabolism and ATG8 stability in Arabidopsis. Accelerated senescence in ACBP3-OEs is dependent on salicylic acid but not jasmonic acid signaling. © 2010 American Society of Plant Biologists.
 
ISSN1040-4651
2012 Impact Factor: 9.251
2012 SCImago Journal Rankings: 5.043
 
DOIhttp://dx.doi.org/10.1105/tpc.110.075333
 
PubMed Central IDPMC2899868
 
ISI Accession Number IDWOS:000279253200007
Funding AgencyGrant Number
Research Grants Council of the Hong Kong Special Administrative Region, ChinaHKU7047/07M
University of Hong Kong10208034
National Science FoundationEPS 0236913
MCB 0455318
DBI 0521587
Kansas Technology Enterprise Corporation
Kansas IDeA Network of Biomedical Research Excellence (INBRE) of the National Institutes of HealthP20RR16475
Kansas State University
Funding Information:

We thank M. Roth (Kansas Lipidomics Research Center) for lipid profiling, the ABRC for provision of npr1-5 and acbp3 mutant seeds, D. X. Xie (Tsinghua University) for the coi1-2 mutant, and S. F. Chen (University of Hong Kong) for provision of HPLC. This work was supported by the Research Grants Council of the Hong Kong Special Administrative Region, China (Project HKU7047/07M), and the University of Hong Kong (Project 10208034, postdoctoral fellowship to S.X. and studentships to W.G., Q.-F.C., S.-X.Z., S.-W.C., and J.M.). Lipid profiling was performed at the Kansas Lipidomics Research Center, where method development and instrument acquisition were supported by the National Science Foundation (EPS 0236913, MCB 0455318, and DBI 0521587), the Kansas Technology Enterprise Corporation, the Kansas IDeA Network of Biomedical Research Excellence (INBRE) of the National Institutes of Health (P20RR16475), and Kansas State University.

 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorXiao, S
 
dc.contributor.authorGao, W
 
dc.contributor.authorChen, QF
 
dc.contributor.authorChan, SW
 
dc.contributor.authorZheng, SX
 
dc.contributor.authorMa, J
 
dc.contributor.authorWang, M
 
dc.contributor.authorWelti, R
 
dc.contributor.authorChye, ML
 
dc.date.accessioned2010-05-07T04:03:57Z
 
dc.date.available2010-05-07T04:03:57Z
 
dc.date.issued2010
 
dc.description.abstractIn Arabidopsis thaliana, a family of six genes (ACBP1 to ACBP6) encodes acyl-CoA binding proteins (ACBPs). Investigations on ACBP3 reported here show its upregulation upon dark treatment and in senescing rosettes. Transgenic Arabidopsis overexpressing ACBP3 (ACBP3-OEs) displayed accelerated leaf senescence, whereas an acbp3 T-DNA insertional mutant and ACBP3 RNA interference transgenic Arabidopsis lines were delayed in dark-induced leaf senescence. Acyl-CoA and lipid profiling revealed that the overexpression of ACBP3 led to an increase in acyl-CoA and phosphatidylethanolamine (PE) levels, whereas ACBP3 downregulation reduced PE content. Moreover, significant losses in phosphatidylcholine (PC) and phosphatidylinositol, and gains in phosphatidic acid (PA), lysophospholipids, and oxylipin-containing galactolipids (arabidopsides) were evident in 3-week-old dark-treated and 6-week-old premature senescing ACBP3-OEs. Such accu-mulation of PA and arabidopsides (A, B, D, E, and G) resulting from lipid peroxidation in ACBP3-OEs likely promoted leaf senescence. The N-terminal signal sequence/transmembrane domain in ACBP3 was shown to be essential in ACBP3-green fluorescent protein targeting and in promoting senescence. Observations that recombinant ACBP3 binds PC, PE, and unsaturated acyl-CoAs in vitro and that ACBP3 overexpression enhances degradation of the autophagy (ATG)-related protein ATG8 and disrupts autophagosome formation suggest a role for ACBP3 as a phospholipid binding protein involved in the regulation of leaf senescence by modulating membrane phospholipid metabolism and ATG8 stability in Arabidopsis. Accelerated senescence in ACBP3-OEs is dependent on salicylic acid but not jasmonic acid signaling. © 2010 American Society of Plant Biologists.
 
dc.description.naturepublished_or_final_version
 
dc.identifier.citationPlant Cell, 2010, v. 22 n. 5, p. 1463-1482 [How to Cite?]
DOI: http://dx.doi.org/10.1105/tpc.110.075333
 
dc.identifier.doihttp://dx.doi.org/10.1105/tpc.110.075333
 
dc.identifier.eissn1532-298X
 
dc.identifier.epage1482
 
dc.identifier.hkuros171737
 
dc.identifier.isiWOS:000279253200007
Funding AgencyGrant Number
Research Grants Council of the Hong Kong Special Administrative Region, ChinaHKU7047/07M
University of Hong Kong10208034
National Science FoundationEPS 0236913
MCB 0455318
DBI 0521587
Kansas Technology Enterprise Corporation
Kansas IDeA Network of Biomedical Research Excellence (INBRE) of the National Institutes of HealthP20RR16475
Kansas State University
Funding Information:

We thank M. Roth (Kansas Lipidomics Research Center) for lipid profiling, the ABRC for provision of npr1-5 and acbp3 mutant seeds, D. X. Xie (Tsinghua University) for the coi1-2 mutant, and S. F. Chen (University of Hong Kong) for provision of HPLC. This work was supported by the Research Grants Council of the Hong Kong Special Administrative Region, China (Project HKU7047/07M), and the University of Hong Kong (Project 10208034, postdoctoral fellowship to S.X. and studentships to W.G., Q.-F.C., S.-X.Z., S.-W.C., and J.M.). Lipid profiling was performed at the Kansas Lipidomics Research Center, where method development and instrument acquisition were supported by the National Science Foundation (EPS 0236913, MCB 0455318, and DBI 0521587), the Kansas Technology Enterprise Corporation, the Kansas IDeA Network of Biomedical Research Excellence (INBRE) of the National Institutes of Health (P20RR16475), and Kansas State University.

 
dc.identifier.issn1040-4651
2012 Impact Factor: 9.251
2012 SCImago Journal Rankings: 5.043
 
dc.identifier.issue5
 
dc.identifier.pmcidPMC2899868
 
dc.identifier.pmid20442372
 
dc.identifier.scopuseid_2-s2.0-77954392870
 
dc.identifier.spage1463
 
dc.identifier.urihttp://hdl.handle.net/10722/57626
 
dc.identifier.volume22
 
dc.language.isoeng
 
dc.publisherAmerican Society of Plant Biologists. The Journal's web site is located at http://www.plantcell.org
 
dc.publisher.placeUnited States
 
dc.relation.ispartofPlant Cell
 
dc.relation.referencesReferences in Scopus
 
dc.rightsThe Plant Cell. Copyright © American Society of Plant Biologists
 
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License
 
dc.subjectBiology - botany
 
dc.subjectBiology - biochemistry
 
dc.titleOverexpression of Arabidopsis acyl-CoA binding protein ACBP3 promotes starvation-induced and age-dependent leaf senescence
 
dc.typeArticle
 
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<contributor.author>Zheng, SX</contributor.author>
<contributor.author>Ma, J</contributor.author>
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Author Affiliations
  1. Kansas State University
  2. The University of Hong Kong