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Biophys J, July 1999, p. 248-257, Vol. 77, No. 1

Heteromeric Assembly of Kv2.1 with Kv9.3: Effect on the State Dependence of Inactivation

Daniel Kerschensteiner and Martin Stocker

Molekulare Biologie Neuronaler Signale, Max-Planck-Institut für Experimentelle Medizin, D-37075 Göttingen, Germany

Modulatory alpha -subunits of Kv channels remain electrically silent after homomeric expression. Their interactions with Kv2 alpha -subunits via the amino-terminal domain promote the assembly of heteromeric functional channels. The kinetic features of these heteromers differ from those of Kv2 homomers, suggesting a distinct role in electrical signaling. This study investigates biophysical properties of channels emerging from the coexpression of Kv2.1 with the modulatory alpha -subunit Kv9.3. Changes relative to homomeric Kv2.1 concern activation, deactivation, inactivation, and recovery from inactivation. A detailed description of Kv2.1/Kv9.3 inactivation is presented. Kv2.1/Kv9.3 heteromers inactivate in a fast and complete fashion from intermediate closed states, but in a slow and incomplete manner from open states. Intermediate closed states of channel gating can be approached through partial activation or deactivation, according to a proposed qualitative model. These transitions are rate-limiting for Kv2.1/Kv9.3 inactivation. Finally, based on the kinetic description, we propose a putative function for Kv2.1/Kv9.3 heteromers in rat heart.

Biophys J, July 1999, p. 248-257, Vol. 77, No. 1
© 1999 by the Biophysical Society   0006-3495/99/07/248/10  $2.00


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