Tue G. Banke

TL;DR: It is suggested that AMPA receptor peak response open probability can be increased by PKA through phosphorylation of GluR1 Ser845.

TL;DR: Analysis of the sequence of single‐channel open and closed intervals shows that both NR2A‐ and NR2B‐containing receptors undergo multiple conformational changes prior to opening of the channel, with at least one of these steps being faster for NR1/NR2A thanNR2B.

TL;DR: Findings from crystallographic and electrophysiological studies of the mechanism of activation of an AMPA-subtype glutamate receptor ion channel are reported, showing that the GluR2 ligand-binding core can adopt a range of lig and-dependent conformational states, which in turn control the open probability of discrete subconductance states of the intact ion channel.

TL;DR: CaMKII phosphorylation of GluA1-Ser831 decreases the activation energy for an intrasubunit conformational change that regulates the conductance of the receptor when the channel pore opens, which underlies the observation that phospho- Ser831 increases the frequency of openings to larger conductances rather than altering unitary conductance.

TL;DR: A new working model of receptor activation is proposed that can account for macroscopic as well as microscopic NMDA receptor properties and suggests that NR1 and NR2B subunits, respectively, undergo a fast and slow agonist-dependent conformational change that precedes opening of the pore.