Structure of the Arabidopsis Glutamate Receptor-like Channel GLR3.2 Ligand-Binding Domain

Gangwar, S.P.; Green, Marriah N.; Michard, Erwan; Simon, Alexander A.; Feijó, José A.; Sobolevsky, Alexander I.

doi:10.1016/j.str.2020.09.006

Cited by 25 publications

(16 citation statements)

References 66 publications

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“…Instead, a water molecule occupies the void, where it is stabilized by hydrogen bonds with the hydroxymethyl side chain of serine, the guanidinium group of R16, the amide group of Q135, and the backbone carbonyl oxygen of D136 (Figure S6B). Water molecules played a similar role in the binding of glycine to the LBDs of GLR3.2 and GLR3.3 (Alfieri et al, 2020;Gangwar et al, 2021). Altogether, these data illustrate how the ligandbinding pocket of GLRs evolved to bind differently sized amino acids by exploiting the same interactions for binding the conserved amino acid core and adjusting the fit of the side chains with water.…”

Section: Llmentioning

confidence: 65%

“…The key interactions with agonists and binding residues are conserved among iGluRs and GLRs (Alfieri et al, 2020;Gangwar et al, 2021). For all three agonists, the guanidinium group of R92 (R577 in the full-length GLR3.4) and the backbone amines of T87 and F139 are hydrogen bonded to the carboxyl group of the ligand, while the backbone carbonyl oxygen of D85, the hydroxyl groups of T87 and Y186, and the carboxyl group of E183 coordinate the amino group of the ligand.…”

Section: Llmentioning

confidence: 99%

“…The molecularly oriented approaches to harness GLR function rely on the detailed knowledge of GLR structural organization. Recent studies of the GLR3.2 and GLR3.3 ligand-binding ll domains (LBDs), from the model organism Arabidopsis thaliana, provided the first glimpse of the fragment of GLR structure responsible for ligand binding (Alfieri et al, 2020;Gangwar et al, 2021). GLR3.2 and GLR3.3 LBD structures identified similar overall folds to iGluRs' LBD structures, with the distinct features in the ligand-binding pocket that are responsible for the promiscuous GLR activation by various amino acids.…”

Section: Introductionmentioning

confidence: 99%

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Structure of the Arabidopsis thaliana glutamate receptor-like channel GLR3.4

et al. 2021

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Section: Llmentioning

confidence: 65%

Section: Llmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Structure of the Arabidopsis thaliana glutamate receptor-like channel GLR3.4

et al. 2021

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“…Numerous iGluRs have been identified in nonmammals (Mayer and Jegla, 2018), such as insects (Benton et al, 2009;Li et al, 2016b;Prieto-Godino et al, 2016), worms (Maricq et al, 1995), plants (Lam et al, 1998), and single-cell organisms (Chen et al, 1999a;Lomash et al, 2013;Alberstein et al, 2015). The subunits in those organisms share their modular domain organization and architecture with the mammalian receptors, and the structures of isolated ABDs are similar (Mayer et al, 2001;Lomash et al, 2013;Alberstein et al, 2015;Han et al, 2015b;Li et al, 2016b;Alfieri et al, 2020;Stroebel and Paoletti, 2021;Gangwar et al, 2021). However, there are substantial differences in pharmacology, gating kinetics (Lomash et al, 2013;Alberstein et al, 2015;Prieto-Godino et al, 2017), and the role of auxiliary subunits (Zheng et al, 2004;Walker et al, 2006;Wang et al, 2012;Han et al, 2015b).…”

Section: A Subunit Stoichiometry and Domain Organizationmentioning

confidence: 99%

Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels

Hansen¹,

Wollmuth²,

Bowie³

et al. 2021

Pharmacol Rev

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445

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“…Initial notice of a calcium-voltage-change association was made in the context of the wound/foraging response in the model plant Arabidopsis. Upon wounding the signaling molecule glutamate gets released to the extracellular space 16 , faced by ligand-binding site of GLRs 17 , 18 . The Arabidopsis genome harbors 20 GLRs.…”

Section: Introductionmentioning

confidence: 99%

Ether anesthetics prevents touch-induced trigger hair calcium-electrical signals excite the Venus flytrap

Scherzer

Huang

Iosip

et al. 2022

Sci Rep

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Plants do not have neurons but operate transmembrane ion channels and can get electrical excited by physical and chemical clues. Among them the Venus flytrap is characterized by its peculiar hapto-electric signaling. When insects collide with trigger hairs emerging the trap inner surface, the mechanical stimulus within the mechanosensory organ is translated into a calcium signal and an action potential (AP). Here we asked how the Ca2+ wave and AP is initiated in the trigger hair and how it is feed into systemic trap calcium-electrical networks. When Dionaea muscipula trigger hairs matures and develop hapto-electric excitability the mechanosensitive anion channel DmMSL10/FLYC1 and voltage dependent SKOR type Shaker K+ channel are expressed in the sheering stress sensitive podium. The podium of the trigger hair is interface to the flytrap’s prey capture and processing networks. In the excitable state touch stimulation of the trigger hair evokes a rise in the podium Ca2+ first and before the calcium signal together with an action potential travel all over the trap surface. In search for podium ion channels and pumps mediating touch induced Ca2+ transients, we, in mature trigger hairs firing fast Ca2+ signals and APs, found OSCA1.7 and GLR3.6 type Ca2+ channels and ACA2/10 Ca2+ pumps specifically expressed in the podium. Like trigger hair stimulation, glutamate application to the trap directly evoked a propagating Ca2+ and electrical event. Given that anesthetics affect K+ channels and glutamate receptors in the animal system we exposed flytraps to an ether atmosphere. As result propagation of touch and glutamate induced Ca2+ and AP long-distance signaling got suppressed, while the trap completely recovered excitability when ether was replaced by fresh air. In line with ether targeting a calcium channel addressing a Ca2+ activated anion channel the AP amplitude declined before the electrical signal ceased completely. Ether in the mechanosensory organ did neither prevent the touch induction of a calcium signal nor this post stimulus decay. This finding indicates that ether prevents the touch activated, glr3.6 expressing base of the trigger hair to excite the capture organ.

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Structure of the Arabidopsis Glutamate Receptor-like Channel GLR3.2 Ligand-Binding Domain

Cited by 25 publications

References 66 publications

Structure of the Arabidopsis thaliana glutamate receptor-like channel GLR3.4

Structure of the Arabidopsis thaliana glutamate receptor-like channel GLR3.4

Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels

Ether anesthetics prevents touch-induced trigger hair calcium-electrical signals excite the Venus flytrap

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