{"@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/1360004235993850112.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1128/mcb.01017-15"}},{"identifier":{"@type":"URI","@value":"https://journals.asm.org/doi/pdf/10.1128/MCB.01017-15"}},{"identifier":{"@type":"URI","@value":"https://www.tandfonline.com/doi/pdf/10.1128/MCB.01017-15"}},{"identifier":{"@type":"PMID","@value":"26787842"}}],"resourceType":"学術雑誌論文(journal article)","dc:title":[{"@value":"Scaffold Protein Ahk1, Which Associates with Hkr1, Sho1, Ste11, and Pbs2, Inhibits Cross Talk Signaling from the Hkr1 Osmosensor to the Kss1 Mitogen-Activated Protein Kinase"}],"description":[{"notation":[{"@value":"In the budding yeast Saccharomyces cerevisiae, osmostress activates the Hog1 mitogen-activated protein kinase (MAPK), which regulates diverse osmoadaptive responses. Hkr1 is a large, highly glycosylated, single-path transmembrane protein that is a putative osmosensor in one of the Hog1 upstream pathways termed the HKR1 subbranch. The extracellular region of Hkr1 contains both a positive and a negative regulatory domain. However, the function of the cytoplasmic domain of Hkr1 (Hkr1-cyto) is unknown. Here, using a mass spectrometric method, we identified a protein, termed Ahk1 (Associated with Hkr1), that binds to Hkr1-cyto. Deletion of the AHK1 gene (in the absence of other Hog1 upstream branches) only partially inhibited osmostress-induced Hog1 activation. In contrast, Hog1 could not be activated by constitutively active mutants of the Hog1 pathway signaling molecules Opy2 or Ste50 in ahk1Δ cells, whereas robust Hog1 activation occurred in AHK1(+) cells. In addition to Hkr1-cyto binding, Ahk1 also bound to other signaling molecules in the HKR1 subbranch, including Sho1, Ste11, and Pbs2. Although osmotic stimulation of Hkr1 does not activate the Kss1 MAPK, deletion of AHK1 allowed Hkr1 to activate Kss1 by cross talk. Thus, Ahk1 is a scaffold protein in the HKR1 subbranch and prevents incorrect signal flow from Hkr1 to Kss1."}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1380004235993850368","@type":"Researcher","foaf:name":[{"@value":"Akiko Nishimura"}],"jpcoar:affiliationName":[{"@value":"Division of Molecular Cell Signaling, Institute of Medical Science, University of Tokyo, Tokyo, Japan"},{"@value":"Department of Biological Sciences, Graduate School of Science, University of Tokyo, Tokyo, Japan"}]},{"@id":"https://cir.nii.ac.jp/crid/1030285133841815424","@type":"Researcher","personIdentifier":[{"@type":"KAKEN_RESEARCHERS","@value":"70508366"},{"@type":"NRID","@value":"1000070508366"},{"@type":"NRID","@value":"9000004259352"},{"@type":"NRID","@value":"9000010511897"}],"foaf:name":[{"@value":"Katsuyoshi Yamamoto"}],"jpcoar:affiliationName":[{"@value":"Division of Molecular Cell Signaling, Institute of Medical Science, University of Tokyo, Tokyo, Japan"}]},{"@id":"https://cir.nii.ac.jp/crid/1380004235993850113","@type":"Researcher","foaf:name":[{"@value":"Masaaki Oyama"}],"jpcoar:affiliationName":[{"@value":"Medical Proteomics Laboratory, Institute of Medical Science, University of Tokyo, Tokyo, Japan"}]},{"@id":"https://cir.nii.ac.jp/crid/1420001326236059648","@type":"Researcher","personIdentifier":[{"@type":"KAKEN_RESEARCHERS","@value":"80401256"},{"@type":"NRID","@value":"1000080401256"},{"@type":"NRID","@value":"9000261672693"},{"@type":"NRID","@value":"9000343410040"},{"@type":"NRID","@value":"9000391969551"},{"@type":"NRID","@value":"9000391969577"},{"@type":"NRID","@value":"9000411203042"},{"@type":"NRID","@value":"9000402600006"},{"@type":"NRID","@value":"9000399833812"},{"@type":"NRID","@value":"9000347092203"},{"@type":"NRID","@value":"9000391969977"},{"@type":"NRID","@value":"9000318581051"},{"@type":"RESEARCHMAP","@value":"https://researchmap.jp/res_1589"}],"foaf:name":[{"@value":"Hiroko Kozuka-Hata"}],"jpcoar:affiliationName":[{"@value":"Medical Proteomics Laboratory, Institute of Medical Science, University of Tokyo, Tokyo, Japan"}]},{"@id":"https://cir.nii.ac.jp/crid/1380004235993850112","@type":"Researcher","foaf:name":[{"@value":"Haruo Saito"}],"jpcoar:affiliationName":[{"@value":"Division of Molecular Cell Signaling, Institute of Medical Science, University of Tokyo, Tokyo, Japan"},{"@value":"Department of Biological Sciences, Graduate School of Science, University of Tokyo, Tokyo, Japan"}]},{"@id":"https://cir.nii.ac.jp/crid/1420282801198092544","@type":"Researcher","personIdentifier":[{"@type":"KAKEN_RESEARCHERS","@value":"50272498"},{"@type":"NRID","@value":"1000050272498"},{"@type":"NRID","@value":"9000003798741"},{"@type":"NRID","@value":"9000318141023"},{"@type":"NRID","@value":"9000242714877"},{"@type":"NRID","@value":"9000001545725"},{"@type":"NRID","@value":"9000023214549"},{"@type":"NRID","@value":"9000283347433"},{"@type":"RESEARCHMAP","@value":"https://researchmap.jp/50272498"}],"foaf:name":[{"@value":"Kazuo Tatebayashi"}],"jpcoar:affiliationName":[{"@value":"Division of Molecular Cell Signaling, Institute of Medical Science, University of Tokyo, Tokyo, Japan"},{"@value":"Department of Biological Sciences, Graduate School of Science, University of Tokyo, Tokyo, Japan"}]}],"publication":{"publicationIdentifier":[{"@type":"EISSN","@value":"10985549"}],"prism:publicationName":[{"@value":"Molecular and Cellular Biology"}],"dc:publisher":[{"@value":"Informa UK Limited"}],"prism:publicationDate":"2016-04-01","prism:volume":"36","prism:number":"7","prism:startingPage":"1109","prism:endingPage":"1123"},"reviewed":"false","dc:rights":["https://journals.asm.org/non-commercial-tdm-license"],"url":[{"@id":"https://journals.asm.org/doi/pdf/10.1128/MCB.01017-15"},{"@id":"https://www.tandfonline.com/doi/pdf/10.1128/MCB.01017-15"}],"createdAt":"2016-01-20","modifiedAt":"2023-03-17","foaf:topic":[{"@id":"https://cir.nii.ac.jp/all?q=Mitogen-Activated%20Protein%20Kinase%20Kinases","dc:title":"Mitogen-Activated Protein Kinase Kinases"},{"@id":"https://cir.nii.ac.jp/all?q=Cytoplasm","dc:title":"Cytoplasm"},{"@id":"https://cir.nii.ac.jp/all?q=Saccharomyces%20cerevisiae%20Proteins","dc:title":"Saccharomyces cerevisiae Proteins"},{"@id":"https://cir.nii.ac.jp/all?q=Membrane%20Proteins","dc:title":"Membrane Proteins"},{"@id":"https://cir.nii.ac.jp/all?q=Saccharomyces%20cerevisiae","dc:title":"Saccharomyces cerevisiae"},{"@id":"https://cir.nii.ac.jp/all?q=MAP%20Kinase%20Kinase%20Kinases","dc:title":"MAP Kinase Kinase Kinases"},{"@id":"https://cir.nii.ac.jp/all?q=Protein%20Structure,%20Tertiary","dc:title":"Protein Structure, Tertiary"},{"@id":"https://cir.nii.ac.jp/all?q=Osmoregulation","dc:title":"Osmoregulation"},{"@id":"https://cir.nii.ac.jp/all?q=Nuclear%20Matrix-Associated%20Proteins","dc:title":"Nuclear Matrix-Associated Proteins"},{"@id":"https://cir.nii.ac.jp/all?q=Osmotic%20Pressure","dc:title":"Osmotic Pressure"},{"@id":"https://cir.nii.ac.jp/all?q=Mitogen-Activated%20Protein%20Kinases","dc:title":"Mitogen-Activated Protein Kinases"},{"@id":"https://cir.nii.ac.jp/all?q=Carrier%20Proteins","dc:title":"Carrier Proteins"},{"@id":"https://cir.nii.ac.jp/all?q=Protein%20Binding","dc:title":"Protein Binding"},{"@id":"https://cir.nii.ac.jp/all?q=Signal%20Transduction","dc:title":"Signal Transduction"}],"project":[{"@id":"https://cir.nii.ac.jp/crid/1040000782256423808","@type":"Project","projectIdentifier":[{"@type":"KAKEN","@value":"25440042"},{"@type":"JGN","@value":"JP25440042"},{"@type":"URI","@value":"https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-25440042/"}],"notation":[{"@language":"ja","@value":"酵母ＭＡＰＫ経路特異性制御機構の解明"},{"@language":"en","@value":"Regulation mechanism of MAPK pathway specificity in yeast"}]},{"@id":"https://cir.nii.ac.jp/crid/1040282257175895808","@type":"Project","projectIdentifier":[{"@type":"KAKEN","@value":"24370053"},{"@type":"JGN","@value":"JP24370053"},{"@type":"URI","@value":"https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-24370053/"}],"notation":[{"@language":"ja","@value":"膜蛋白質の多量体形成と動的相互作用を介した高浸透圧感知機構"},{"@language":"en","@value":"Osmosensing mechanisms via oligomerization and dynamic interactions of the membrane proteins"}]},{"@id":"https://cir.nii.ac.jp/crid/1040282257284500608","@type":"Project","projectIdentifier":[{"@type":"KAKEN","@value":"26505001"},{"@type":"JGN","@value":"JP26505001"},{"@type":"URI","@value":"https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-26505001/"}],"notation":[{"@language":"ja","@value":"定量リン酸化プロテオミクスによる膠芽腫幹細胞mTORシグナルの阻害攪乱機構の解明"},{"@language":"en","@value":"Quantitative phosphoproteomic analysis of mTOR signaling perturbation in glioblastoma stem cells"}]}],"relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1360011142933996928","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"High-Quality Binary Protein Interaction Map of the Yeast Interactome Network"}]},{"@id":"https://cir.nii.ac.jp/crid/1360011144170114944","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Osmostress‐induced gene expression – a model to understand how stress‐activated protein kinases (<scp>SAPK</scp>s) regulate transcription"}]},{"@id":"https://cir.nii.ac.jp/crid/1360011144599888768","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Dynamic Control of Yeast MAP Kinase Network by Induced Association and Dissociation between the Ste50 Scaffold and the Opy2 Membrane Anchor"}]},{"@id":"https://cir.nii.ac.jp/crid/1360283690829065856","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"FBXL21 Regulates Oscillation of the Circadian Clock through Ubiquitination and Stabilization of Cryptochromes"}]},{"@id":"https://cir.nii.ac.jp/crid/1360285707268252288","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Comprehensive Identification of Nuclear and Cytoplasmic TNRC6A-Associating Proteins"}]},{"@id":"https://cir.nii.ac.jp/crid/1360285710970390912","@type":"Article","resourceType":"学術雑誌論文(journal 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2K"}]},{"@id":"https://cir.nii.ac.jp/crid/1360292619036821376","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Requirement of STE50 for Osmostress-Induced Activation of the STE11 Mitogen-Activated Protein Kinase Kinase Kinase in the High-Osmolarity Glycerol Response Pathway"}]},{"@id":"https://cir.nii.ac.jp/crid/1360298754838230784","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Two activating phosphorylation sites of Pbs2 MAP2K in the yeast HOG pathway are differentially dephosphorylated by four PP2C phosphatases Ptc1–Ptc4"}]},{"@id":"https://cir.nii.ac.jp/crid/1360565169653101568","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Response to Hyperosmotic Stress"}]},{"@id":"https://cir.nii.ac.jp/crid/1360567183385306880","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Osmosensing and scaffolding functions of the oligomeric four-transmembrane domain osmosensor Sho1"}]},{"@id":"https://cir.nii.ac.jp/crid/1360574094604487168","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Ste5 tethers multiple protein kinases in the MAP kinase cascade required for mating in S. cerevisiae"}]},{"@id":"https://cir.nii.ac.jp/crid/1360574095047575168","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"The Ste5 Scaffold Directs Mating Signaling by Catalytically Unlocking the Fus3 MAP Kinase for Activation"}]},{"@id":"https://cir.nii.ac.jp/crid/1360574096140804224","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"A docking site determining specificity of Pbs2 MAPKK for Ssk2/Ssk22 MAPKKKs in the yeast HOG pathway"}]},{"@id":"https://cir.nii.ac.jp/crid/1360588379383630080","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"A cryptic promoter in the exon of HKR1 drives expression of a truncated form of Hkr1 in Saccharomyces cerevisiae"}]},{"@id":"https://cir.nii.ac.jp/crid/1360848660888681344","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Yeast Osmosensors Hkr1 and Msb2 Activate the Hog1 MAPK Cascade by Different Mechanisms"}]},{"@id":"https://cir.nii.ac.jp/crid/1360855567861221760","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Signalling scaffolds and local organization of cellular behaviour"}]},{"@id":"https://cir.nii.ac.jp/crid/1360855569777105024","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"MAPK Hog1 closes the <i>S. cerevisiae</i> glycerol channel Fps1 by phosphorylating and displacing its positive regulators"}]},{"@id":"https://cir.nii.ac.jp/crid/1360861705599579392","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Comprehensive characterization of the Hsp70 interactome reveals novel client proteins and interactions mediated by posttranslational modifications"}]},{"@id":"https://cir.nii.ac.jp/crid/1361137045354543360","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Unique and Redundant Roles for HOG MAPK Pathway Components as Revealed by Whole-Genome Expression Analysis"}]},{"@id":"https://cir.nii.ac.jp/crid/1361137045879818880","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"An Osmosensing Signal Transduction Pathway in Yeast"}]},{"@id":"https://cir.nii.ac.jp/crid/1361137046253582336","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"The Ste5p scaffold"}]},{"@id":"https://cir.nii.ac.jp/crid/1361418518525872256","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Roles of glycerol and glycerol-3-phosphate dehydrogenase (NAD+) in acquired osmotolerance of Saccharomyces cerevisiae"}]},{"@id":"https://cir.nii.ac.jp/crid/1361418519562644736","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Time-Dependent Quantitative Multicomponent Control of the G\n            <sub>1</sub>\n            -S Network by the Stress-Activated Protein Kinase Hog1 upon Osmostress"}]},{"@id":"https://cir.nii.ac.jp/crid/1361418520051236608","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Role of the Unfolded Protein Response in Regulating the Mucin-Dependent Filamentous-Growth Mitogen-Activated Protein Kinase Pathway"}]},{"@id":"https://cir.nii.ac.jp/crid/1361699994401648128","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Regulatable promoters of Saccharomyces cerevisiae: comparison of transcriptional activity and their use for heterologous expression"}]},{"@id":"https://cir.nii.ac.jp/crid/1361699995872973056","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Osmotic Stress Signaling and Osmoadaptation in Yeasts"}]},{"@id":"https://cir.nii.ac.jp/crid/1361699996123107072","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Cleavage of the signaling mucin Msb2 by the aspartyl protease Yps1 is required for MAPK activation in yeast"}]},{"@id":"https://cir.nii.ac.jp/crid/1361981471291563008","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Adaptor functions of Cdc42, Ste50, and Sho1 in the yeast osmoregulatory HOG MAPK pathway"}]},{"@id":"https://cir.nii.ac.jp/crid/1361981471380603776","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Phylogenetic relationships among yeasts of the ? complex? determined from multigene sequence analyses"}]},{"@id":"https://cir.nii.ac.jp/crid/1362262943626638336","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"A two-component system that regulates an osmosensing MAP kinase cascade in yeast"}]},{"@id":"https://cir.nii.ac.jp/crid/1362262945493869184","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Nbp2 targets the Ptc1‐type 2C Ser/Thr phosphatase to the HOG MAPK pathway"}]},{"@id":"https://cir.nii.ac.jp/crid/1362262946008747264","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Activation of the yeast SSK2 MAP kinase kinase kinase by the SSK1 two-component response regulator"}]},{"@id":"https://cir.nii.ac.jp/crid/1362262946078584320","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"A signaling mucin at the head of the Cdc42- and MAPK-dependent filamentous growth pathway in yeast"}]},{"@id":"https://cir.nii.ac.jp/crid/1362544418612086272","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"[14] Cloning genes by complementation in yeast"}]},{"@id":"https://cir.nii.ac.jp/crid/1362544418874033024","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"The HOG Pathway Dictates the Short-Term Translational Response after Hyperosmotic Shock"}]},{"@id":"https://cir.nii.ac.jp/crid/1362544419675086464","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Yeast HOG1 MAP Kinase Cascade Is Regulated by a Multistep Phosphorelay Mechanism in the SLN1–YPD1–SSK1 “Two-Component” Osmosensor"}]},{"@id":"https://cir.nii.ac.jp/crid/1362544419974534656","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Phosphorylation of the MEKK Ste11p by the PAK-like kinase Ste20p is required for MAP kinase signaling in vivo"}]},{"@id":"https://cir.nii.ac.jp/crid/1362825893569534080","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Osmotic Activation of the HOG MAPK Pathway via Ste11p MAPKKK: Scaffold Role of Pbs2p MAPKK"}]},{"@id":"https://cir.nii.ac.jp/crid/1362825893650557696","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Binding the Atypical RA Domain of Ste50p to the Unfolded Opy2p Cytoplasmic Tail Is Essential for the High-Osmolarity Glycerol Pathway"}]},{"@id":"https://cir.nii.ac.jp/crid/1362825895532132096","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Phosphorylated Ssk1 Prevents Unphosphorylated Ssk1 from Activating the Ssk2 Mitogen-Activated Protein Kinase Kinase Kinase in the Yeast High-Osmolarity Glycerol Osmoregulatory Pathway"}]},{"@id":"https://cir.nii.ac.jp/crid/1362825895802194944","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Two Binding Orientations for Peptides to the Src SH3 Domain: Development of a General Model for SH3-Ligand Interactions"}]},{"@id":"https://cir.nii.ac.jp/crid/1362825895927727488","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Regulation of Cell Cycle Progression by Swe1p and Hog1p Following Hypertonic Stress"}]},{"@id":"https://cir.nii.ac.jp/crid/1362825895936851200","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Control of high osmolarity signalling in the yeast <i>Saccharomyces cerevisiae</i>"}]},{"@id":"https://cir.nii.ac.jp/crid/1363107368432344448","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Differential input by Ste5 scaffold and Msg5 phosphatase route a MAPK cascade to multiple outcomes"}]},{"@id":"https://cir.nii.ac.jp/crid/1363107368786368384","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Phosphorylation of Hsl1 by Hog1 leads to a G2 arrest essential for cell survival at high osmolarity"}]},{"@id":"https://cir.nii.ac.jp/crid/1363107369067291648","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Transmembrane mucins Hkr1 and Msb2 are putative osmosensors in the SHO1 branch of yeast HOG pathway"}]},{"@id":"https://cir.nii.ac.jp/crid/1363107370536801280","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"GPD1, which encodes glycerol-3-phosphate dehydrogenase, is essential for growth under osmotic stress in Saccharomyces cerevisiae, and its expression is regulated by the high-osmolarity glycerol response pathway."}]},{"@id":"https://cir.nii.ac.jp/crid/1363107370651096960","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"MAP Kinases"}]},{"@id":"https://cir.nii.ac.jp/crid/1363107371251949184","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Scaffold Proteins: Hubs for Controlling the Flow of Cellular Information"}]},{"@id":"https://cir.nii.ac.jp/crid/1363388843390197760","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Dual Role for Membrane Localization in Yeast MAP Kinase Cascade Activation and Its Contribution to Signaling Fidelity"}]},{"@id":"https://cir.nii.ac.jp/crid/1363388844189218304","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Structurally unique interaction of RBD-like and PH domains is crucial for yeast pheromone 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