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    Cover picture: All eukaryotic ionotropic glutamate receptors, including AMPA and NMDA receptors, have a transmembrane segment, the M4 segment, that is positioned peripherally to the pore domain. For AMPA receptors, the M4 segment mediates receptor oligomerization, whereas for NMDA receptor subunits, GluN1 and GluN2A, the extracellular end of M4 mediates receptor gating, probably reflecting a strong interaction with its own S1-M1 linker (see Research Article by Amin et al., 661–680).

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ISSN 0022-1295
EISSN 1540-7748
In this Issue

Research News

New JGP paper explains sexual dimorphism and tissue-specific activity of TRPV4.

Viewpoint

Sula and Wallace explore evidence supporting a role for a novel interaction motif in the gating of prokaryotic sodium channels.

Article

The pharmacological effects of inhaled anesthetics on ion channel function are poorly understood. Sand et al. analyze macroscopic gating of the prokaryotic voltage-gated sodium channel, NaChBac, using a six-state kinetic scheme and demonstrate that isoflurane modulates microscopic gating properties.

Vascular smooth muscle tone can be regulated by angiotensin II, which enhances TRPV4 channel activity via AKAP150-bound protein kinase C. Tajada et al. show that the effect of AKAP150 on TRPV4 channels is inversely proportional to the distance between them, which varies with sex and arterial bed.

AMPA and NMDA receptors are ionotropic glutamate receptors that make fundamental contributions to synaptic activity in the brain in different ways. Amin et al. show that their respective M4 segments, located on the periphery of their pore domains, contribute to their functional diversity.

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