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

Marriah N. Green, Shanti Pal Gangwar, Erwan Michard, Alexander A. Simon, Maria Teresa Portes, Juan Barbosa-Caro, Michael M. Wudick, Michael A. Lizzio, Oleg Klykov, Maria V. Yelshanskaya, José A. Feijó, Alexander I. Sobolevsky

Research output: Contribution to journalArticlepeer-review

39 Scopus citations


Glutamate receptor-like channels (GLRs) play vital roles in various physiological processes in plants, such as wound response, stomatal aperture control, seed germination, root development, innate immune response, pollen tube growth, and morphogenesis. Despite the importance of GLRs, knowledge about their molecular organization is limited. Here we use X-ray crystallography and single-particle cryo-EM to solve structures of the Arabidopsis thaliana GLR3.4. Our structures reveal the tetrameric assembly of GLR3.4 subunits into a three-layer domain architecture, reminiscent of animal ionotropic glutamate receptors (iGluRs). However, the non-swapped arrangement between layers of GLR3.4 domains, binding of glutathione through S-glutathionylation of cysteine C205 inside the amino-terminal domain clamshell, unique symmetry, inter-domain interfaces, and ligand specificity distinguish GLR3.4 from representatives of the iGluR family and suggest distinct features of the GLR gating mechanism. Our work elaborates on the principles of GLR architecture and symmetry and provides a molecular template for deciphering GLR-dependent signaling mechanisms in plants.

Original languageEnglish (US)
Pages (from-to)3216-3226.e8
JournalMolecular Cell
Issue number15
StatePublished - Aug 5 2021
Externally publishedYes


  • Arabidopsis thaliana
  • GLR
  • X-ray crystallography
  • cryo-EM
  • glutamate receptor
  • glutathione
  • glutathionylation
  • iGluR
  • plant
  • structure

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology


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