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Cryo-EM structure of the Potassium channel AKT1 mutant from Arabidopsis thalianaCryo-EM structure of the Potassium channel AKT1 mutant from Arabidopsis thaliana
Structural highlights
FunctionAKT1_ARATH Highly selective inward-rectifying potassium channel that mediate potassium uptake by plant roots in response to low K(+) conditions, by a calcium-, CBL-, and CIPK-dependent pathway. Positively regulated by phosphorylation by CIPK23. Negatively regulated by a kinase-independent regulatory mechanism involving a competing direct binding of CBL10. Involved in the stomatal regulation by monitoring the turgor pressure in guard cells. Assuming opened or closed conformations in response to the voltage difference across the membrane, the channel is activated by hyperpolarization. May interact with the cytoskeleton or with regulatory proteins.[1] [2] [3] [4] [5] Publication Abstract from PubMedThe voltage-gated potassium channel AKT1 is responsible for primary K(+) uptake in Arabidopsis roots. AKT1 is functionally activated through phosphorylation and negatively regulated by a potassium channel alpha-subunit AtKC1. However, the molecular basis for the modulation mechanism remains unclear. Here we report the structures of AKT1, phosphorylated-AKT1, a constitutively-active variant, and AKT1-AtKC1 complex. AKT1 is assembled in 2-fold symmetry at the cytoplasmic domain. Such organization appears to sterically hinder the reorientation of C-linkers during ion permeation. Phosphorylated-AKT1 adopts an alternate 4-fold symmetric conformation at cytoplasmic domain, which indicates conformational changes associated with symmetry switch during channel activation. To corroborate this finding, we perform structure-guided mutagenesis to disrupt the dimeric interface and identify a constitutively-active variant Asp379Ala mediates K(+) permeation independently of phosphorylation. This variant predominantly adopts a 4-fold symmetric conformation. Furthermore, the AKT1-AtKC1 complex assembles in 2-fold symmetry. Together, our work reveals structural insight into the regulatory mechanism for AKT1. Structural basis for the activity regulation of a potassium channel AKT1 from Arabidopsis.,Lu Y, Yu M, Jia Y, Yang F, Zhang Y, Xu X, Li X, Yang F, Lei J, Wang Y, Yang G Nat Commun. 2022 Sep 27;13(1):5682. doi: 10.1038/s41467-022-33420-8. PMID:36167696[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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