Alexander I. Sobolevsky

TL;DR: The crystal structure of the α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA)-sensitive, homotetrameric, rat GluA2 receptor is reported at 3.6 Å resolution in complex with a competitive antagonist to exploit mechanisms of ion channel activation, desensitization and inhibition by non-competitive antagonists and pore blockers.

TL;DR: It is shown here that the unprecedented large statistics obtained by uPAINT on single cells reveal local diffusion properties of specific proteins, either in distinct membrane compartments of adherent cells or in neuronal synapses.

TL;DR: Crystal structures are now available for the ligand-binding domain, but the structure of the ion channel itself remains unknown, and differences are emerging in the glutamate receptor ion channel.

TL;DR: The crystal structure of rat TRPV6 is reported at 3.25 Å resolution and a Ca2+ permeation mechanism is proposed on the basis of crystallographically identified cation-binding sites at the pore axis and extracellular vestibule, providing a structural foundation for understanding the regulation of epithelial Ca2+.

TL;DR: Cryo-electron microscopy is used to solve the structures of AMPA receptor–auxiliary subunit complexes in the apo, antagonist- and agonist-bound states and determine the iris-like mechanism of ion channel opening, providing a framework for understanding gating across the family of ionotropic glutamate receptors and the role of AMpa receptors in excitatory neurotransmission.