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http://purl.uniprot.org/citations/26764375http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26764375http://www.w3.org/2000/01/rdf-schema#comment"Dark respiration causes an increase in leaf CO2 concentration (Ci), and the continuing increases in atmospheric [CO2] further increases Ci. Elevated leaf CO2 concentration causes stomatal pores to close. Here, we demonstrate that high intracellular CO2/HCO3 (-) enhances currents mediated by the Arabidopsis thaliana guard cell S-type anion channel SLAC1 upon coexpression of any one of the Arabidopsis protein kinases OST1, CPK6, or CPK23 in Xenopus laevis oocytes. Split-ubiquitin screening identified the PIP2;1 aquaporin as an interactor of the βCA4 carbonic anhydrase, which was confirmed in split luciferase, bimolecular fluorescence complementation, and coimmunoprecipitation experiments. PIP2;1 exhibited CO2 permeability. Mutation of PIP2;1 in planta alone was insufficient to impair CO2- and abscisic acid-induced stomatal closing, likely due to redundancy. Interestingly, coexpression of βCA4 and PIP2;1 with OST1-SLAC1 or CPK6/23-SLAC1 in oocytes enabled extracellular CO2 enhancement of SLAC1 anion channel activity. An inactive PIP2;1 point mutation was identified that abrogated water and CO2 permeability and extracellular CO2 regulation of SLAC1 activity. These findings identify the CO2-permeable PIP2;1 as key interactor of βCA4 and demonstrate functional reconstitution of extracellular CO2 signaling to ion channel regulation upon coexpression of PIP2;1, βCA4, SLAC1, and protein kinases. These data further implicate SLAC1 as a bicarbonate-responsive protein contributing to CO2 regulation of S-type anion channels."xsd:string
http://purl.uniprot.org/citations/26764375http://purl.org/dc/terms/identifier"doi:10.1105/tpc.15.00637"xsd:string
http://purl.uniprot.org/citations/26764375http://purl.uniprot.org/core/author"Hu H."xsd:string
http://purl.uniprot.org/citations/26764375http://purl.uniprot.org/core/author"Qin X."xsd:string
http://purl.uniprot.org/citations/26764375http://purl.uniprot.org/core/author"Wang C."xsd:string
http://purl.uniprot.org/citations/26764375http://purl.uniprot.org/core/author"Xu D."xsd:string
http://purl.uniprot.org/citations/26764375http://purl.uniprot.org/core/author"Schroeder J.I."xsd:string
http://purl.uniprot.org/citations/26764375http://purl.uniprot.org/core/author"Boron W.F."xsd:string
http://purl.uniprot.org/citations/26764375http://purl.uniprot.org/core/author"Rappel W.J."xsd:string
http://purl.uniprot.org/citations/26764375http://purl.uniprot.org/core/author"Zeise B."xsd:string
http://purl.uniprot.org/citations/26764375http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/26764375http://purl.uniprot.org/core/name"Plant Cell"xsd:string
http://purl.uniprot.org/citations/26764375http://purl.uniprot.org/core/pages"568-582"xsd:string
http://purl.uniprot.org/citations/26764375http://purl.uniprot.org/core/title"Reconstitution of CO2 Regulation of SLAC1 Anion Channel and Function of CO2-Permeable PIP2;1 Aquaporin as CARBONIC ANHYDRASE4 Interactor."xsd:string
http://purl.uniprot.org/citations/26764375http://purl.uniprot.org/core/volume"28"xsd:string
http://purl.uniprot.org/citations/26764375http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/26764375
http://purl.uniprot.org/citations/26764375http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/26764375
http://purl.uniprot.org/uniprot/#_B3H6F9-mappedCitation-26764375http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/26764375
http://purl.uniprot.org/uniprot/#_F4JGW8-mappedCitation-26764375http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/26764375
http://purl.uniprot.org/uniprot/#_Q38872-mappedCitation-26764375http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/26764375
http://purl.uniprot.org/uniprot/#_P43286-mappedCitation-26764375http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/26764375
http://purl.uniprot.org/uniprot/#_Q94CE4-mappedCitation-26764375http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/26764375
http://purl.uniprot.org/uniprot/#_Q9LD83-mappedCitation-26764375http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/26764375
http://purl.uniprot.org/uniprot/#_Q940H6-mappedCitation-26764375http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/26764375