Regulation of sensory neuron-specific acid-sensing ion channel 3 by the adaptor protein NHERF-1

doi:10.1074/jbc.M509669200

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Papers In Press, published online ahead of print October 17, 2005
J. Biol. Chem, 10.1074/jbc.M509669200
Submitted on September 1, 2005
Accepted on October 17, 2005

Regulation of sensory neuron-specific acid-sensing ion channel 3 by the adaptor protein NHERF-1

Emmanuel Deval, Valérie Friend, Cécile Thirant, Miguel Salinas, Martine Jodar, Michel Lazdunski, and Eric Lingueglia

IPMC-UMR 6097, Valbonne - Sophia Antipolis 06560

Corresponding Author: lingueglia{at}ipmc.cnrs.fr

Acid-Sensing Ion channels (ASICs) are cationic channels activated by extracellular protons. The ASIC3 subunit is largely expressed in the peripheral nervous system where it contributes to pain perception and to some aspects of mechanosensation. We report here a PDZ-dependent and protein kinase C-modulated association between ASIC3 and the adaptor protein NHERF-1. We show that NHERF-1 and ASIC3 are co-expressed in DRG neurons. NHERF-1 enhances the ASIC3 peak current in heterologous cells, including F-11 DRG cells, by increasing the amount of channel at the plasma membrane. Perhaps more importantly, we show that the plateau current of ASIC3 can be dramatically increased (10- to 30-fold) by association with NHERF-1, leading to a significant sustained current at pH 6.6. In the presence of NHERF-1, the ASIC3 subcellular localization is modified and the channel co-localizes with ezrin, a member of the ezrin-radixin-moesin family of actin-binding proteins, providing the first direct link between ASIC3 and the cortical cytoskeleton. Given the importance of the ASIC3 sustained current in nociceptor excitability, it is likely that NHERF-1 participates in channel functions associated with nociception and mechanosensation.

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