J. R. Bankston

This study identifies how LRMP inhibits cAMP-induced potentiation of HCN4 channels by disrupting intramolecular signaling, revealing isoform-specific interaction domains.

The paper investigates the conformational dynamics of ASIC1a termini using FRET methods, finding no close interaction at rest and modest movement during desensitization, suggesting a revised model for RIPK1 binding during acidosis.

This study identifies structural features of lipids that modulate ASICs, showing that negatively charged head groups and specific arginine interactions are critical for potentiation.

This paper identifies two ER proteins, LRMP and IRAG, that modulate HCN4 channel function differently, with LRMP inhibiting and IRAG enhancing HCN4 activity in a cAMP-independent manner.

This study identifies two distinct sites on ASIC3 critical for Stomatin binding and regulation, showing that Stomatin affects ASIC3 gating through the transmembrane domain rather than surface expression.