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Cover Image
Cover Image
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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Research News
TRPV4 in the battle of the sexes
New JGP paper explains sexual dimorphism and tissue-specific activity of TRPV4.
Viewpoint
Interpreting the functional role of a novel interaction motif in prokaryotic sodium channels
Sula and Wallace explore evidence supporting a role for a novel interaction motif in the gating of prokaryotic sodium channels.
Article
Isoflurane modulates activation and inactivation gating of the prokaryotic Na+ channel NaChBac
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.
Distance constraints on activation of TRPV4 channels by AKAP150-bound PKCα in arterial myocytes
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.
Divergent roles of a peripheral transmembrane segment in AMPA and NMDA receptors
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.
