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Biophys J, April 1999, p. 2004-2017, Vol. 76, No. 4
Department of Physiology, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6085 USA
Voltage-gated K+ channels are tetrameric, but
how the four subunits assemble is not known. We analyzed inactivation
kinetics and peak current levels elicited for a variety of wild-type
and mutant Kv1.3 subunits, expressed singly, in combination, and as tandem constructs, to show that 1) the dominant pathway involves a
dimerization of dimers, and 2) dimer-dimer interaction may involve interaction sites that differ from those involved in monomer-monomer association. Moreover, using nondenaturing gel electrophoresis, we
detected dimers and tetramers, but not trimers, in the translation reaction of Kv1.3 monomers.
Biophys J, April 1999, p. 2004-2017, Vol. 76, No. 4
© 1999 by the Biophysical Society 0006-3495/99/04/2004/14 $2.00
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