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Article: GmSAL1 Hydrolyzes Inositol-1,4,5-Trisphosphate and Regulates Stomatal Closure in Detached Leaves and Ion Compartmentalization in Plant Cells

TitleGmSAL1 Hydrolyzes Inositol-1,4,5-Trisphosphate and Regulates Stomatal Closure in Detached Leaves and Ion Compartmentalization in Plant Cells
Authors
Issue Date2013
PublisherPublic Library of Science. The Journal's web site is located at http://www.plosone.org/home.action
Citation
PLOS One, 2013, v. 8 n. 10, article no. e78181 How to Cite?
AbstractInositol polyphosphatases are important regulators since they control the catabolism of phosphoinositol derivatives, which are often signaling molecules for cellular processes. Here we report on the characterization of one of their members in soybean, GmSAL1. In contrast to the substrate specificity of its Arabidopsis homologues (AtSAL1 and AtSAL2), GmSAL1 only hydrolyzes inositol-1,4,5-trisphosphate (IP3) but not inositol-1,3,4-trisphosphate or inositol-1,4-bisphosphate.The ectopic expression of GmSAL1 in transgenic Arabidopsis thaliana led to a reduction in IP3 signals, which was inferred from the reduction in the cytoplasmic signals of the in vivo biomarker pleckstrin homology domain–green florescent protein fusion protein and the suppression of abscisic acid-induced stomatal closure. At the cellular level, the ectopic expression of GmSAL1 in transgenic BY-2 cells enhanced vacuolar Na+ compartmentalization and therefore could partially alleviate salinity stress.
Persistent Identifierhttp://hdl.handle.net/10722/198652
ISSN
2015 Impact Factor: 3.057
2015 SCImago Journal Rankings: 1.395
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorKu, Yen_US
dc.contributor.authorKoo, NSen_US
dc.contributor.authorLi, FWen_US
dc.contributor.authorLi, Men_US
dc.contributor.authorWang, Hen_US
dc.contributor.authorTsai, Sen_US
dc.contributor.authorSun, Fen_US
dc.contributor.authorLim, BLen_US
dc.contributor.authorKo, WHen_US
dc.contributor.authorLam, HMen_US
dc.date.accessioned2014-07-07T08:33:35Z-
dc.date.available2014-07-07T08:33:35Z-
dc.date.issued2013en_US
dc.identifier.citationPLOS One, 2013, v. 8 n. 10, article no. e78181en_US
dc.identifier.issn1932-6203en_US
dc.identifier.urihttp://hdl.handle.net/10722/198652-
dc.description.abstractInositol polyphosphatases are important regulators since they control the catabolism of phosphoinositol derivatives, which are often signaling molecules for cellular processes. Here we report on the characterization of one of their members in soybean, GmSAL1. In contrast to the substrate specificity of its Arabidopsis homologues (AtSAL1 and AtSAL2), GmSAL1 only hydrolyzes inositol-1,4,5-trisphosphate (IP3) but not inositol-1,3,4-trisphosphate or inositol-1,4-bisphosphate.The ectopic expression of GmSAL1 in transgenic Arabidopsis thaliana led to a reduction in IP3 signals, which was inferred from the reduction in the cytoplasmic signals of the in vivo biomarker pleckstrin homology domain–green florescent protein fusion protein and the suppression of abscisic acid-induced stomatal closure. At the cellular level, the ectopic expression of GmSAL1 in transgenic BY-2 cells enhanced vacuolar Na+ compartmentalization and therefore could partially alleviate salinity stress.en_US
dc.languageengen_US
dc.publisherPublic Library of Science. The Journal's web site is located at http://www.plosone.org/home.actionen_US
dc.relation.ispartofPLOS Oneen_US
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.titleGmSAL1 Hydrolyzes Inositol-1,4,5-Trisphosphate and Regulates Stomatal Closure in Detached Leaves and Ion Compartmentalization in Plant Cellsen_US
dc.typeArticleen_US
dc.identifier.emailLim, BL: bllim@hkucc.hku.hken_US
dc.identifier.authorityLim, BL=rp00744en_US
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1371/journal.pone.0078181en_US
dc.identifier.pmid24167607-
dc.identifier.pmcidPMC3805524-
dc.identifier.hkuros229139en_US
dc.identifier.volume8en_US
dc.identifier.isiWOS:000326034500067-
dc.publisher.placeUnited Statesen_US

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