Annexin II light chain p11 promotes functional expression of acid-sensing ion channel ASIC1a

doi:10.1074/jbc.M505981200

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Papers In Press, published online ahead of print September 16, 2005
J. Biol. Chem, 10.1074/jbc.M505981200
Submitted on June 1, 2005
Revised on September 15, 2005
Accepted on September 16, 2005

Annexin II light chain p11 promotes functional expression of acid-sensing ion channel ASIC1a

Emmanuelle Donier, Francois Rugiero, Kenji Okuse, and John N. Wood

Biology, UCL, London, UK WC1E 6BT

Corresponding Author: j.wood{at}ucl.ac.uk

Acid-sensing ion channels (ASICs) have been implicated in a wide variety of physiological functions. We have used a rat dorsal root ganglion cDNA library in a yeast 2-hybrid assay to identify sensory neuron proteins that interact with ASICs. We found that the annexin II light chain p11 physically interacts with the N-terminus of ASIC1a but not other ASIC isoforms. Immunoprecipitation studies confirm an interaction between p11 and ASIC1 in rat dorsal root ganglion neurons in vivo. Co-expression of p11 and ASIC1a in CHO-K1 cells led to a 2-fold increase in expression of the ion channel at the cell membrane, as judged either by membrane-associated immunoreactivity or cell surface biotinylation. Consistent with these findings ASIC1a peak currents in transfected CHO-K1 cells were upregulated 2-fold in the presence of p11, whilst ASIC3 mediated currents were unaffected by p11 expression. Neither the pH dependence of activation or rates of desensitisation were altered by p11, suggesting its primary role in regulating ASIC1a activity is to enhance cell surface expression of ASIC1a. These data demonstrate that p11, already known to traffic members of the voltage-gated sodium and potassium channel families, as well as Transient Receptor Potential and chloride channels, also plays a selective role in enhancing ASIC1a functional expression.

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