{"@context":{"@vocab":"https://cir.nii.ac.jp/schema/1.0/","rdfs":"http://www.w3.org/2000/01/rdf-schema#","dc":"http://purl.org/dc/elements/1.1/","dcterms":"http://purl.org/dc/terms/","foaf":"http://xmlns.com/foaf/0.1/","prism":"http://prismstandard.org/namespaces/basic/2.0/","cinii":"http://ci.nii.ac.jp/ns/1.0/","datacite":"https://schema.datacite.org/meta/kernel-4/","ndl":"http://ndl.go.jp/dcndl/terms/","jpcoar":"https://github.com/JPCOAR/schema/blob/master/2.0/"},"@id":"https://cir.nii.ac.jp/crid/1360004233253176832.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1021/pr201127u"}},{"identifier":{"@type":"URI","@value":"https://pubs.acs.org/doi/pdf/10.1021/pr201127u"}},{"identifier":{"@type":"PMID","@value":"22182420"}}],"resourceType":"学術雑誌論文(journal article)","dc:title":[{"@value":"Phosphoproteome Exploration Reveals a Reformatting of Cellular Processes in Response to Low Sterol Biosynthetic Capacity in <i>Arabidopsis</i>"}],"description":[{"notation":[{"@value":"Sterols are membrane-bound isoprenoid lipids that are required for cell viability and growth. In plants, it is generally assumed that 3-hydroxy-3-methylglutaryl-CoA-reductase (HMGR) is a key element of their biosynthesis, but the molecular regulation of that pathway is largely unknown. In an attempt to identify regulators of the biosynthetic flux from acyl-CoA toward phytosterols, we compared the membrane phosphoproteome of wild-type Arabidopsis thaliana and of a mutant being deficient in HMGR1. We performed a N-terminal labeling of microsomal peptides with a trimethoxyphenyl phosphonium (TMPP) derivative, followed by a quantitative assessment of phosphopeptides with a spectral counting method. TMPP derivatization of peptides resulted in an improved LC-MS/MS detection due to increased hydrophobicity in chromatography and ionization efficiency in electrospray. The phosphoproteome coverage was 40% higher with this methodology. We further found that 31 proteins were in a different phosphorylation state in the hmgr1-1 mutant as compared with the wild-type. One-third of these proteins were identified based on novel phosphopeptides. This approach revealed that phosphorylation changes in the Arabidopsis membrane proteome targets major cellular processes such as transports, calcium homeostasis, photomorphogenesis, and carbohydrate synthesis. A reformatting of these processes appears to be a response of a genetically reduced sterol biosynthesis."}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1380004233253176838","@type":"Researcher","foaf:name":[{"@value":"Anne Berna"}],"jpcoar:affiliationName":[{"@value":"Institut de Biologie Moléculaire\rdes Plantes, Centre National de la Recherche Scientifique-Unité\rPropre de Recherche 2357, Université de Strasbourg, 28 rue Goethe, 67083 Strasbourg, France"}]},{"@id":"https://cir.nii.ac.jp/crid/1380004233253176834","@type":"Researcher","foaf:name":[{"@value":"Alain Van Dorsselaer"}],"jpcoar:affiliationName":[{"@value":"Laboratoire de Spectrométrie\rde Masse Bio-Organique, Institut Pluridisciplinaire Hubert Curien,\rDépartement Sciences Analytiques et Interactions Ioniques et\rBiomoléculaires, Université de Strasbourg, Unité Mixte de Recherche 7178 du CNRS, 25 rue Becquerel,\r67087 Strasbourg, France"}]},{"@id":"https://cir.nii.ac.jp/crid/1380004233253176836","@type":"Researcher","foaf:name":[{"@value":"Toshiya Muranaka"}],"jpcoar:affiliationName":[{"@value":"Cell\rTechnology Laboratory, Department\rof Biotechnology, Osaka University, 2-1Yamadaoka,\rSuita, Osaka 565-087, Japan"}]},{"@id":"https://cir.nii.ac.jp/crid/1380004233253176832","@type":"Researcher","foaf:name":[{"@value":"Shigeo Yoshida"}],"jpcoar:affiliationName":[{"@value":"Riken, Wako-shi,\rSaitama 351-0198, Japan"}]},{"@id":"https://cir.nii.ac.jp/crid/1380004233253176833","@type":"Researcher","foaf:name":[{"@value":"Sebastien Gallien"}],"jpcoar:affiliationName":[{"@value":"Laboratoire de Spectrométrie\rde Masse Bio-Organique, Institut Pluridisciplinaire Hubert Curien,\rDépartement Sciences Analytiques et Interactions Ioniques et\rBiomoléculaires, Université de Strasbourg, Unité Mixte de Recherche 7178 du CNRS, 25 rue Becquerel,\r67087 Strasbourg, France"}]},{"@id":"https://cir.nii.ac.jp/crid/1380004233253176960","@type":"Researcher","foaf:name":[{"@value":"Hubert Schaller"}],"jpcoar:affiliationName":[{"@value":"Institut de Biologie Moléculaire\rdes Plantes, Centre National de la Recherche Scientifique-Unité\rPropre de Recherche 2357, Université de Strasbourg, 28 rue Goethe, 67083 Strasbourg, France"}]},{"@id":"https://cir.nii.ac.jp/crid/1380004233253176837","@type":"Researcher","foaf:name":[{"@value":"Dimitri Heintz"}],"jpcoar:affiliationName":[{"@value":"Institut de Biologie Moléculaire\rdes Plantes, Centre National de la Recherche Scientifique-Unité\rPropre de Recherche 2357, Université de Strasbourg, 28 rue Goethe, 67083 Strasbourg, France"}]},{"@id":"https://cir.nii.ac.jp/crid/1380004233253176841","@type":"Researcher","foaf:name":[{"@value":"Christine Schaeffer"}],"jpcoar:affiliationName":[{"@value":"Laboratoire de Spectrométrie\rde Masse Bio-Organique, Institut Pluridisciplinaire Hubert Curien,\rDépartement Sciences Analytiques et Interactions Ioniques et\rBiomoléculaires, Université de Strasbourg, Unité Mixte de Recherche 7178 du CNRS, 25 rue Becquerel,\r67087 Strasbourg, France"}]},{"@id":"https://cir.nii.ac.jp/crid/1380004233253176835","@type":"Researcher","foaf:name":[{"@value":"Vincent Compagnon"}],"jpcoar:affiliationName":[{"@value":"Institut de Biologie Moléculaire\rdes Plantes, Centre National de la Recherche Scientifique-Unité\rPropre de Recherche 2357, Université de Strasbourg, 28 rue Goethe, 67083 Strasbourg, France"}]},{"@id":"https://cir.nii.ac.jp/crid/1380004233253176839","@type":"Researcher","foaf:name":[{"@value":"Masashi Suzuki"}],"jpcoar:affiliationName":[{"@value":"Riken, Plant Metabolic Diversity Department,\rPlant Science Center, Yokohama,\rKanagawa 230-0045, Japan"}]},{"@id":"https://cir.nii.ac.jp/crid/1380004233253176840","@type":"Researcher","foaf:name":[{"@value":"Thomas J. Bach"}],"jpcoar:affiliationName":[{"@value":"Institut de Biologie Moléculaire\rdes Plantes, Centre National de la Recherche Scientifique-Unité\rPropre de Recherche 2357, Université de Strasbourg, 28 rue Goethe, 67083 Strasbourg, France"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"15353893"},{"@type":"EISSN","@value":"15353907"}],"prism:publicationName":[{"@value":"Journal of Proteome Research"}],"dc:publisher":[{"@value":"American Chemical Society (ACS)"}],"prism:publicationDate":"2012-01-11","prism:volume":"11","prism:number":"2","prism:startingPage":"1228","prism:endingPage":"1239"},"reviewed":"false","url":[{"@id":"https://pubs.acs.org/doi/pdf/10.1021/pr201127u"}],"createdAt":"2011-12-19","modifiedAt":"2023-04-17","foaf:topic":[{"@id":"https://cir.nii.ac.jp/all?q=Proteome","dc:title":"Proteome"},{"@id":"https://cir.nii.ac.jp/all?q=Arabidopsis%20Proteins","dc:title":"Arabidopsis Proteins"},{"@id":"https://cir.nii.ac.jp/all?q=Cell%20Membrane","dc:title":"Cell Membrane"},{"@id":"https://cir.nii.ac.jp/all?q=Molecular%20Sequence%20Data","dc:title":"Molecular Sequence Data"},{"@id":"https://cir.nii.ac.jp/all?q=Arabidopsis","dc:title":"Arabidopsis"},{"@id":"https://cir.nii.ac.jp/all?q=Phytosterols","dc:title":"Phytosterols"},{"@id":"https://cir.nii.ac.jp/all?q=Phosphoproteins","dc:title":"Phosphoproteins"},{"@id":"https://cir.nii.ac.jp/all?q=Plant%20Leaves","dc:title":"Plant Leaves"},{"@id":"https://cir.nii.ac.jp/all?q=Microsomes","dc:title":"Microsomes"},{"@id":"https://cir.nii.ac.jp/all?q=Mutation","dc:title":"Mutation"},{"@id":"https://cir.nii.ac.jp/all?q=Hydroxymethylglutaryl%20CoA%20Reductases","dc:title":"Hydroxymethylglutaryl CoA Reductases"},{"@id":"https://cir.nii.ac.jp/all?q=Amino%20Acid%20Sequence","dc:title":"Amino Acid Sequence"},{"@id":"https://cir.nii.ac.jp/all?q=Signal%20Transduction","dc:title":"Signal 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Kinase"}]},{"@id":"https://cir.nii.ac.jp/crid/1362262945572081408","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Novel subsets of the Arabidopsis plasmalemma phosphoproteome identify phosphorylation sites in secondary active transporters"}]},{"@id":"https://cir.nii.ac.jp/crid/1362262945648680832","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Two SNF1-Related Protein Kinases from Spinach Leaf Phosphorylate and Inactivate 3-Hydroxy-3-Methylglutaryl-Coenzyme A Reductase, Nitrate Reductase, and Sucrose Phosphate Synthase in Vitro1"}]},{"@id":"https://cir.nii.ac.jp/crid/1362262945788092672","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Inhibition of Squalene Synthase and Squalene Epoxidase in Tobacco Cells Triggers an Up-Regulation of 3-Hydroxy-3-Methylglutaryl Coenzyme A Reductase"}]},{"@id":"https://cir.nii.ac.jp/crid/1362544418464604416","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"The Proteomic Response of <i>Mycobacterium smegmatis</i> to Anti-Tuberculosis Drugs Suggests Targeted Pathways"}]},{"@id":"https://cir.nii.ac.jp/crid/1362544419540204160","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"The\n                    <i>Arabidopsis</i>\n                    Nitrate Transporter NRT1.8 Functions in Nitrate Removal from the Xylem Sap and Mediates Cadmium Tolerance"}]},{"@id":"https://cir.nii.ac.jp/crid/1362544420657548032","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Nitrate transporters and peptide transporters"}]},{"@id":"https://cir.nii.ac.jp/crid/1362544420871778560","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Quantitative Proteomics Analysis of the Secretory 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