Acidosis-induced activation of anion channel SLAH3 in the flooding-related stress response of Arabidopsis

Lehmann, Julian; Jørgensen, Morten; Fratz, Stefanie; Müller, Heike M.; Kusch, Jana; Scherzer, Sönke; Navarro‐Retamal, Carlos; Mayer, Dominik; Böhm, Jennifer; Konrad, Kai R.; Terpitz, Ulrich; Drèyer, Ingo; Mueller, Thomas D.; Sauer, Markus; Hedrich, Rainer; Geiger, Dietmar; Maierhofer, Tobias

doi:10.1016/j.cub.2021.06.018

Cited by 34 publications

(18 citation statements)

References 86 publications

(129 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Phosphorylation has been widely reported to modulate the function of ion channels or transporters in plants. For example, phosphorylation modulates the activity of SLAH/SLAC anion channels through stoichiometry change 27 , 28 . And phosphorylation by CIPK23 and CBL1 may activate HAK5 by releasing the autoinhibitory domain 29 .…”

Section: Discussionmentioning

confidence: 99%

Structural basis for the activity regulation of a potassium channel AKT1 from Arabidopsis

Jia

et al. 2022

Nat Commun

View full text Add to dashboard Cite

The 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 α-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.

show abstract

Section: Discussionmentioning

confidence: 99%

Structural basis for the activity regulation of a potassium channel AKT1 from Arabidopsis

Jia

et al. 2022

Nat Commun

View full text Add to dashboard Cite

show abstract

“…The latter is exemplified by the regulation of anion channels in guard cells that convey adaptation to drought and osmotic stress. Here, the SLAC1 channel as well as related SLAH channels are subject to regulation by the combined function of several CDPKs and CBL-CIPK complexes (Geiger et al, 2010;Brandt et al, 2012Brandt et al, , 2015Scherzer et al, 2012;Maierhofer et al, 2014;Lehmann et al, 2021). Currently, it remains to be clarified if these multiple kinases provide alternative paths of ion channel activation or if they also convey additive levels of ion transport enhancement.…”

Section: Getting the Message: Components And Mechanisms Decoding Stre...mentioning

confidence: 99%

Ca²⁺ signaling in plant responses to abiotic stresses

Dong¹,

Wallrad²,

Almutairi

et al. 2022

JIPB

102

View full text Add to dashboard Cite

Adverse variations of abiotic environmental cues that deviate from an optimal range impose stresses to plants. Abiotic stresses severely impede plant physiology and development. Consequently, such stresses dramatically reduce crop yield and negatively impact on ecosystem stability and composition. Physical components of abiotic stresses can be, for example, suboptimal temperature and osmotic perturbations, while representative chemical facets of abiotic stresses can be toxic ions or suboptimal nutrient availability. The sheer complexity of abiotic stresses causes a multitude of diverse components and mechanisms for their sensing and signal transduction. Ca 2+ , as a versatile second messenger, plays multifaceted roles in almost all abiotic stress responses in that, for a certain abiotic stress, Ca 2+ is not only reciprocally connected with its perception, but also multifunctionally ensures subsequent signal transduction. Here, we will focus on salt/osmotic stress and responses to altered nutrient availability as model cases to detail novel insights into the identity of components that link stress perception to Ca 2+ signal formation as well as on new insights into mechanisms of Ca 2+ signal implementation. Finally, we will deduce emerging conceptual consequences of these novel insights and outline arising avenues of future research on the role of Ca 2+ signaling in abiotic stress responses in plants.

show abstract

“…For the reason that ELF3 functions antagonistically with PHYTOCHROME-INTERACTING FACTOR4 (PIF4) in thermomorphogenesis (Raschke et al, 2015), we also found their conversed expression pattern in H. difformis. The proton sensor SLAC1 HOMOLOGUE 3 (SLAH3) (Lehmann et al, 2021), the mechanical stimuli sensor MSCS-LIKE 10 (MSL10) (Tran et al, 2021), and aquaporins Plasma membrane Intrinsic Proteins (PIPs) (Yaneff et al, 2015) are also significantly upregulated in terrestrial conditions. Morphological changes in leaf shape are the most obvious characteristics in heterophyllous plants.…”

Section: Morphological Physiological and Molecular Adaptation Of H Di...mentioning

confidence: 99%

Water wisteria genome reveals environmental adaptation and heterophylly regulation in amphibious plants

Zhao

Yang

et al. 2022

Preprint

View full text Add to dashboard Cite

The phenomenon by which a single plant dramatically changes its leaf shape in response to the surrounding environment is called heterophylly, an ideal model for the study of plant phenotypic adaptation to environment. Hygrophila difformis (Acanthaceae), also known as Water-Wisteria, has recently merged as a model to study heterophylly due to its typical phenotypic plasticity to various ecological factors. Here, we generated a chromosome-level genome of H. difformis (scaffold N50: 57.63Mb, and genome size: 831.53 Mb) and predicted 36,099 protein-coding genes mainly on 15 pseudochromosomes. H. difformis evolved a gene expansion for its acclimation to the amphibious environment. RNA-seq analysis revealed that genes relative to environmental stimuli, leaf development and other processes are elaborated, regulating its morphological and physiological acclimations to the changing environments. Finally, we identified candidate genes under different ecological factors, and illuminated the roles of LATE MERISTEM IDENTITY 1 (LMI1) on the regulation of heterophylly in H. difformis. Our study contributes the first genome and transcriptome for Hygrophila, establishing H. difformis as a model for the relationships of ecological factors and plant morphological features. We provide new insights into the adaptability of plants in evolution, along with potential resources for trait improvement in crops.

show abstract

Acidosis-induced activation of anion channel SLAH3 in the flooding-related stress response of Arabidopsis

Cited by 34 publications

References 86 publications

Structural basis for the activity regulation of a potassium channel AKT1 from Arabidopsis

Structural basis for the activity regulation of a potassium channel AKT1 from Arabidopsis

Ca²⁺ signaling in plant responses to abiotic stresses

Water wisteria genome reveals environmental adaptation and heterophylly regulation in amphibious plants

Contact Info

Product

Resources

About

Acidosis-induced activation of anion channel SLAH3 in the flooding-related stress response of Arabidopsis

Cited by 34 publications

References 86 publications

Structural basis for the activity regulation of a potassium channel AKT1 from Arabidopsis

Structural basis for the activity regulation of a potassium channel AKT1 from Arabidopsis

Ca2+ signaling in plant responses to abiotic stresses

Water wisteria genome reveals environmental adaptation and heterophylly regulation in amphibious plants

Contact Info

Product

Resources

About

Ca²⁺ signaling in plant responses to abiotic stresses