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Control of GluR1 AMPA Receptor Function by cAMP-Dependent Protein Kinase
- T. Banke, D. Bowie, H. Lee, R. Huganir, A. Schousboe, S. Traynelis
- Biology, MedicineThe Journal of Neuroscience
- 1 January 2000
It is suggested that AMPA receptor peak response open probability can be increased by PKA through phosphorylation of GluR1 Ser845.
Subunit‐specific gating controls rat NR1/NR2A and NR1/NR2B NMDA channel kinetics and synaptic signalling profiles
- K. Erreger, S. Dravid, T. Banke, D. Wyllie, S. Traynelis
- Biology, MedicineThe Journal of physiology
- 1 March 2005
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.
Structural basis for partial agonist action at ionotropic glutamate receptors
- R. Jin, T. Banke, M. Mayer, S. Traynelis, E. Gouaux
- Chemistry, MedicineNature Neuroscience
- 1 August 2003
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.
Activation of NR1/NR2B NMDA receptors
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.
Mechanism of Ca2+/calmodulin-dependent kinase II regulation of AMPA receptor gating
- A. Kristensen, Meagan A. Jenkins, +5 authors S. Traynelis
- Biology, MedicineNature Neuroscience
- 1 June 2011
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.
GABAergic Input onto CA3 Hippocampal Interneurons Remains Shunting throughout Development
In hippocampus, GABAA receptor-mediated synaptic input onto stratum lucidum inhibitory interneurons was shunting in nature across the entire developmental age range tested, and pyramidal cell synaptic inhibition demonstrated the well described switch from depolarizing to hyperpolarizing over the same age range.
Tonic activation of group I mGluRs modulates inhibitory synaptic strength by regulating KCC2 activity
It is shown that tonic activation of group I metabotropic glutamate receptors (mGluR1s) regulates inhibitory synaptic strength via modulation of KCC2 function in pyramidal neurons of the hippocampal CA3 area and mGluRs are poised to play a pivotal role in providing a direct interplay between the excitatory and inhibitory systems in the hippocampus.
Protons Trap NR1/NR2B NMDA Receptors in a Nonconducting State
A physical model of proton inhibition is proposed that can describe macroscopic and single-channel properties of NMDA receptor function over a range of pH values.
Activation of TRPA1 by Farnesyl Thiosalicylic Acid
Several compounds are discovered that possess potent, selective TRPA1-activating activity, including several lipid compounds, and it is shown that the mechanism of action of farnesyl thiosalicylic acid differs from that of the reactive electrophilic reagent allylisothiocyanate.
Allosteric interaction between the amino terminal domain and the ligand binding domain of NR2A
It is reported that the fast desensitization of NR1/NR2A receptors is caused by ambient zinc, and that a positive allosteric interaction occurs between the extracellular zinc-binding site located in the amino terminal domain and the glutamate-binding domain of NR2A.