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Plasmodesmal receptor-like kinases identified through analysis of rice cell wall extracted proteins

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dc.contributor.authorJo, Yeonhwa-
dc.contributor.authorCho, Won Kyong-
dc.contributor.authorRim, Yeonggil-
dc.contributor.authorMoon, Juyeon-
dc.contributor.authorChen, Xiong-Yan-
dc.contributor.authorChu, Hyosub-
dc.contributor.authorKim, Cha Young-
dc.contributor.authorPark, Zee-Yong-
dc.contributor.authorLucas, William J.-
dc.contributor.authorKim, Jae-Yean-
dc.date.accessioned2022-12-27T03:10:02Z-
dc.date.available2022-12-27T03:10:02Z-
dc.date.issued2011-01-
dc.identifier.issn0033-183X-
dc.identifier.issn1615-6102-
dc.identifier.urihttps://scholarworks.gnu.ac.kr/handle/sw.gnu/23884-
dc.description.abstractIn plants, plasmodesmata (PD) are intercellular channels that function in both metabolite exchange and the transport of proteins and RNAs. Currently, many of the PD structural and regulatory components remain to be elucidated. Receptor-like kinases (RLKs) belonging to a notably expanded protein family in plants compared to the animal kingdom have been shown to play important roles in plant growth, development, pathogen resistance, and cell death. In this study, cell biological approaches were used to identify potential PD-associated RLK proteins among proteins contained within cell walls isolated from rice callus cultured cells. A total of 15 rice RLKs were investigated to determine their subcellular localization, using an Agrobacterium-mediated transient expression system. Of these six PD-associated RLKs were identified based on their co-localization with a viral movement protein that served as a PD marker, plasmolysis experiments, and subcellular localization at points of wall contact between spongy mesophyll cells. These findings suggest potential PD functions in apoplasmic signaling in response to environmental stimuli and developmental inputs.-
dc.format.extent13-
dc.language영어-
dc.language.isoENG-
dc.publisherSPRINGER WIEN-
dc.titlePlasmodesmal receptor-like kinases identified through analysis of rice cell wall extracted proteins-
dc.typeArticle-
dc.publisher.location오스트리아-
dc.identifier.doi10.1007/s00709-010-0251-4-
dc.identifier.scopusid2-s2.0-78751649203-
dc.identifier.wosid000286466900016-
dc.identifier.bibliographicCitationPROTOPLASMA, v.248, no.1, pp 191 - 203-
dc.citation.titlePROTOPLASMA-
dc.citation.volume248-
dc.citation.number1-
dc.citation.startPage191-
dc.citation.endPage203-
dc.type.docTypeArticle-
dc.description.isOpenAccessY-
dc.description.journalRegisteredClasssci-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalResearchAreaPlant Sciences-
dc.relation.journalResearchAreaCell Biology-
dc.relation.journalWebOfScienceCategoryPlant Sciences-
dc.relation.journalWebOfScienceCategoryCell Biology-
dc.subject.keywordPlusGREEN FLUORESCENT PROTEIN-
dc.subject.keywordPlusTO-CELL-
dc.subject.keywordPlusMOVEMENT PROTEIN-
dc.subject.keywordPlusMACROMOLECULAR TRANSPORT-
dc.subject.keywordPlusSELECTIVE TRAFFICKING-
dc.subject.keywordPlusVIRUS MOVEMENT-
dc.subject.keywordPlusMESSENGER-RNA-
dc.subject.keywordPlusARABIDOPSIS-
dc.subject.keywordPlusTOBACCO-
dc.subject.keywordPlusEXPRESSION-
dc.subject.keywordAuthorPlasmodesmata-
dc.subject.keywordAuthorReceptor-like kinase-
dc.subject.keywordAuthorSymplasmic signaling-
dc.subject.keywordAuthorApoplasmic signaling-
dc.subject.keywordAuthorCell wall proteomics-
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