%0 Journal Article %1 geiger2009activity %A Geiger, Dietmar %A Scherzer, Sönke %A Mumm, Patrick %A Stange, Annette %A Marten, Irene %A Bauer, Hubert %A Ache, Peter %A Matschi, Susanne %A Liese, Anja %A Al-Rasheid, Khaled A S %A Romeis, Tina %A Hedrich, Rainer %C United States %D 2009 %J Proceedings of the National Academy of Sciences of the United States of America %K imported %N 50 %P 21425--21430 %R 10.1073/pnas.0912021106 %T Activity of guard cell anion channel SLAC1 is controlled by drought-stress signaling kinase-phosphatase pair %U https://pubmed.ncbi.nlm.nih.gov/19955405 %V 106 %X In response to drought stress the phytohormone ABA (abscisic acid) induces stomatal closure and, therein, activates guard cell anion channels in a calcium-dependent as well as-independent manner. Two key components of the ABA signaling pathway are the protein kinase OST1 (open stomata 1) and the protein phosphatase ABI1 (ABA insensitive 1). The recently identified guard cell anion channel SLAC1 appeared to be the key ion channel in this signaling pathway but remained electrically silent when expressed heterologously. Using split YFP assays, we identified OST1 as an interaction partner of SLAC1 and ABI1. Upon coexpression of SLAC1 with OST1 in Xenopus oocytes, SLAC1-related anion currents appeared similar to those observed in guard cells. Integration of ABI1 into the SLAC1/OST1 complex, however, prevented SLAC1 activation. Our studies demonstrate that SLAC1 represents the slow, deactivating, weak voltage-dependent anion channel of guard cells controlled by phosphorylation/dephosphorylation.

@article{geiger2009activity, abstract = {In response to drought stress the phytohormone ABA (abscisic acid) induces stomatal closure and, therein, activates guard cell anion channels in a calcium-dependent as well as-independent manner. Two key components of the ABA signaling pathway are the protein kinase OST1 (open stomata 1) and the protein phosphatase ABI1 (ABA insensitive 1). The recently identified guard cell anion channel SLAC1 appeared to be the key ion channel in this signaling pathway but remained electrically silent when expressed heterologously. Using split YFP assays, we identified OST1 as an interaction partner of SLAC1 and ABI1. Upon coexpression of SLAC1 with OST1 in Xenopus oocytes, SLAC1-related anion currents appeared similar to those observed in guard cells. Integration of ABI1 into the SLAC1/OST1 complex, however, prevented SLAC1 activation. Our studies demonstrate that SLAC1 represents the slow, deactivating, weak voltage-dependent anion channel of guard cells controlled by phosphorylation/dephosphorylation.}, added-at = {2024-02-16T13:40:11.000+0100}, address = {United States}, author = {Geiger, Dietmar and Scherzer, Sönke and Mumm, Patrick and Stange, Annette and Marten, Irene and Bauer, Hubert and Ache, Peter and Matschi, Susanne and Liese, Anja and Al-Rasheid, Khaled A S and Romeis, Tina and Hedrich, Rainer}, biburl = {https://www.bibsonomy.org/bibtex/26cbf55543e2e7a1373889cd0a0959b4e/imarten}, comment = {19955405[pmid] PMC2795561[pmcid]}, description = {Activity of guard cell anion channel SLAC1 is controlled by drought-stress signaling kinase-phosphatase pair - PubMed}, doi = {10.1073/pnas.0912021106}, interhash = {235e624f6fad79df5c36138c5579a065}, intrahash = {6cbf55543e2e7a1373889cd0a0959b4e}, issn = {00278424}, journal = {Proceedings of the National Academy of Sciences of the United States of America}, keywords = {imported}, month = dec, number = 50, pages = {21425--21430}, timestamp = {2024-02-16T13:40:11.000+0100}, title = {Activity of guard cell anion channel SLAC1 is controlled by drought-stress signaling kinase-phosphatase pair}, url = {https://pubmed.ncbi.nlm.nih.gov/19955405}, volume = 106, year = 2009 }