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
2011 Impact Factor: 8.987
2011 SCImago Journal Rankings: 1.258
DOIhttp://dx.doi.org/10.1105/tpc.110.075333
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.

PubMed Central IDPMC2899868
ReferencesReferences in Scopus
DC Field
Value
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.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
2011 Impact Factor: 8.987
2011 SCImago Journal Rankings: 1.258
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
Author Affiliations
  1. Kansas State University at Manhattan
  2. The University of Hong Kong