File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Arabidopsis thaliana acyl-CoA-binding protein ACBP6 interacts with plasmodesmata-located protein PDLP8

TitleArabidopsis thaliana acyl-CoA-binding protein ACBP6 interacts with plasmodesmata-located protein PDLP8
Authors
KeywordsAcyl-CoA-binding protein
arabidopsis thaliana
PDLP8
phloem
plasma membrane
plasmodesmata
protein-protein interaction
Issue Date2017
PublisherTaylor & Francis for Society of Plant Signaling and Behavior. The Journal's web site is located at http://www.tandfonline.com/kpsb
Citation
Plant Signaling & Behavior, 2017, v. 12 n. 8, p. e1359365 How to Cite?
AbstractIn Arabidopsis thaliana, six acyl-CoA-binding proteins (ACBPs), designated as AtACBP1 to AtACBP6, have been identified to function in various events related to plant stress and development. The 10-kDa AtACBP6 is the smallest in this protein family, and recombinant AtACBP6 interacts with lipids in vitro by binding to acyl-CoA esters and phosphatidylcholine. Using anti-AtACBP6 antibodies in immunoelectron microscopy, we have localized AtACBP6 in the Arabidopsis phloem. The detection of immunogold grains in the plasmodesmata suggested that AtACBP6 could move from the companion cells to the sieve elements via the plasmodesmata. As AtACBP6 has been identified in a membrane-based interactome analysis to be a potential protein partner of Plasmodesmata-Localized Protein, PDLP8, AtACBP6-PDLP8 interaction was investigated herein utilizing isothermal titration calorimetry, as well as pull-down and bimolecular fluorescence complementation assays (BiFC). Notably, BiFC data revealed that AtACBP6-PDLP8 interaction occurred at the plasma membrane, which was unexpected as AtACBP6 has been previously identified in the cytosol. AtACBP6 expression was generally higher than PDLP8 in β-glucuronidase (GUS) assays on transgenic Arabidopsis transformed with AtACBP6 or PDLP8 promoter-driven GUS, consistent with qRT-PCR and microarray results. Furthermore, western blot analysis using anti-AtACBP6 antibodies showed a reduction in AtACBP6 expression in the pdlp8 T-DNA insertional mutant, suggesting that PDLP8 may possibly influence AtACBP6 accumulation in the sieve elements, probably in the plasmodesmata, where PDLP8 is confined and to where AtACBP6 has been immunodetected.
Persistent Identifierhttp://hdl.handle.net/10722/250608
ISSN
2023 Impact Factor: 2.8
2023 SCImago Journal Rankings: 0.725
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorYe, Z-
dc.contributor.authorChen, QF-
dc.contributor.authorChye, ML-
dc.date.accessioned2018-01-18T04:29:41Z-
dc.date.available2018-01-18T04:29:41Z-
dc.date.issued2017-
dc.identifier.citationPlant Signaling & Behavior, 2017, v. 12 n. 8, p. e1359365-
dc.identifier.issn1559-2316-
dc.identifier.urihttp://hdl.handle.net/10722/250608-
dc.description.abstractIn Arabidopsis thaliana, six acyl-CoA-binding proteins (ACBPs), designated as AtACBP1 to AtACBP6, have been identified to function in various events related to plant stress and development. The 10-kDa AtACBP6 is the smallest in this protein family, and recombinant AtACBP6 interacts with lipids in vitro by binding to acyl-CoA esters and phosphatidylcholine. Using anti-AtACBP6 antibodies in immunoelectron microscopy, we have localized AtACBP6 in the Arabidopsis phloem. The detection of immunogold grains in the plasmodesmata suggested that AtACBP6 could move from the companion cells to the sieve elements via the plasmodesmata. As AtACBP6 has been identified in a membrane-based interactome analysis to be a potential protein partner of Plasmodesmata-Localized Protein, PDLP8, AtACBP6-PDLP8 interaction was investigated herein utilizing isothermal titration calorimetry, as well as pull-down and bimolecular fluorescence complementation assays (BiFC). Notably, BiFC data revealed that AtACBP6-PDLP8 interaction occurred at the plasma membrane, which was unexpected as AtACBP6 has been previously identified in the cytosol. AtACBP6 expression was generally higher than PDLP8 in β-glucuronidase (GUS) assays on transgenic Arabidopsis transformed with AtACBP6 or PDLP8 promoter-driven GUS, consistent with qRT-PCR and microarray results. Furthermore, western blot analysis using anti-AtACBP6 antibodies showed a reduction in AtACBP6 expression in the pdlp8 T-DNA insertional mutant, suggesting that PDLP8 may possibly influence AtACBP6 accumulation in the sieve elements, probably in the plasmodesmata, where PDLP8 is confined and to where AtACBP6 has been immunodetected.-
dc.languageeng-
dc.publisherTaylor & Francis for Society of Plant Signaling and Behavior. The Journal's web site is located at http://www.tandfonline.com/kpsb-
dc.relation.ispartofPlant Signaling & Behavior-
dc.rightsThis is an electronic version of an article published in [include the complete citation information for the final version of the article as published in the print edition of the journal]. [JOURNAL TITLE] is available online at: http://www.informaworld.com/smpp/ with the open URL of your article.-
dc.subjectAcyl-CoA-binding protein-
dc.subjectarabidopsis thaliana-
dc.subjectPDLP8-
dc.subjectphloem-
dc.subjectplasma membrane-
dc.subjectplasmodesmata-
dc.subjectprotein-protein interaction-
dc.titleArabidopsis thaliana acyl-CoA-binding protein ACBP6 interacts with plasmodesmata-located protein PDLP8-
dc.typeArticle-
dc.identifier.emailChye, ML: mlchye@hku.hk-
dc.identifier.authorityChye, ML=rp00687-
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1080/15592324.2017.1359365-
dc.identifier.pmid28786767-
dc.identifier.pmcidPMC5616145-
dc.identifier.scopuseid_2-s2.0-85029600719-
dc.identifier.hkuros283894-
dc.identifier.volume12-
dc.identifier.issue8-
dc.identifier.spagee1359365-
dc.identifier.epagee1359365-
dc.identifier.isiWOS:000428142500016-
dc.publisher.placeUnited States-
dc.identifier.issnl1559-2316-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats