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Honghong Hu

Publications and source records attributed to Honghong Hu.

2 recordsLinked to original sources

Natural Variation in Arabidopsis Cvi-0 Accession Uncovers Regulation of Guard Cell CO2 Signaling by MPK12

Plant gas exchange is regulated by guard cells that form stomatal pores. Stomatal adjustments are crucial for plant survival; they regulate uptake of CO2 for photosynthesis, loss of water and entrance of air pollutants such as ozone. We mapped ozone hypersensitivity, more open stomata and stomatal CO2-insensitivity phenotypes of the Arabidopsis thaliana accession Cvi-0 to a single amino acid substitution in MAP kinase 12 (MPK12). In parallel we showed that stomatal CO2-insensitivity phenotypes of a mutant cis (CO2-insensitive) were caused by a deletion of MPK12. Lack of MPK12 impaired bicarbonate-induced activation of S-type anion channels. We demonstrated that MPK12 interacted with the protein kinase HT1, a central node in guard cell CO2 signaling, and that MPK12 can function as an inhibitor of HT1. These data provide a new function for plant MPKs as protein kinase inhibitors and suggest a mechanism through which guard cell CO2 signaling controls plant water management.

Plant Biology

Reconstitution of CO2 regulation of SLAC1 anion channel and function of CO2-permeable PIP2;1 aquaporin as carbonic anhydrase 4 interactor

Daily dark periods cause an increase in the leaf CO2 concentration (Ci) and the continuing atmospheric [CO2] rise also increases Ci. Elevated Ci causes closing of stomatal pores thus regulating gas exchange of plants. The molecular signaling mechanisms leading to CO2-induced stomatal closure are only partially understood. Here we demonstrate that high intracellular [Formula] enhances currents mediated by the guard cell S-type anion channel SLAC1 when co-expressing either of the protein kinases OST1, CPK6 or CPK23 in Xenopus oocytes. Split-ubiquitin screening identified the PIP2;1 aquaporin as an interactor of the {beta}CA4 carbonic anhydrase, which was confirmed in split luciferase, bimolecular fluorescence complementation and co-immunoprecipitation experiments. PIP2;1 exhibited CO2 permeability. Co-expression of {beta}CA4 and PIP2;1 with OST1-SLAC1 or CPK6/23-SLAC1 enabled extracellular CO2 enhancement of SLAC1 anion channel activity. An inactive PIP2;1 point mutation was identified which abrogated water and CO2 permeability and extracellular CO2 regulation of SLAC1 activity in Xenopus oocytes. These findings identify the CO2-permeable PIP2;1 aquaporin as key interactor of carbonic anhydrases, show functional reconstitution of extracellular CO2 signaling to ion channel regulation and implicate SLAC1 as a bicarbonate-responsive protein in CO2 regulation of S-type anion channels.

Plant Biology