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Articles by Andrew Plested
Atomistic Mechanisms of Calcium Permeation Modulated by Q/R Editing and Selectivity Filter Mutations in GluA2 AMPA Receptors
Abstract GluA2 is a key subunit of AMPA receptor ion channels that is abundantly expressed in the vertebrate brain. Posttranscriptional Q/R editing of GluA2 renders AMPARs nearly impermeable to calcium ions, which is crucial for their normal function. Although previous studies have characterized conductivity and selectivity differences between edited and unedited GluA2 variants and heteromeric receptors incorporating GluA2, the atomistic mechanism remains largely unknown.
NMDA Receptors Singled out for Delayed Activation
In this issue of Neuron, Amin et al. (2021) Amin J. Gochman A. He M. Certain N. Wollmuth L.P. NMDA receptors require multiple pre-opening gating steps for efficient synaptic activity. Neuron. 2021; 109 ( ) : 488-501 recorded single NMDA receptors in synaptic-like conditions to reveal how unreliable coupling between agonist binding and channel opening depends on structured linkers.
Measurements of the Timescale and Conformational Space of AMPA Receptor Desensitization
Abstract Ionotropic glutamate receptors are ligand-gated ion channels that mediate excitatory synaptic transmission in the central nervous system. Desensitization of the α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid subtype after glutamate binding appears critical for brain function and involves rearrangement of the ligand binding domains (LBDs). Recently, several full-length structures of ionotropic glutamate receptors in putative desensitized states were published.
Biophysics of Membrane Protein Signaling
Main Text Membrane proteins such as G protein-coupled receptors, channels, and transporters, as well as variations in the membrane composition itself, drive signaling across cellular membranes. These processes are key for cells to sense their environment, store energy, and respond to stimuli.
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