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Biophys J. 1999 Apr;76(4):2004-17.

Evidence for dimerization of dimers in K+ channel assembly.

Author information

1
Department of Physiology, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6085, USA.

Abstract

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.

PMID:
10096897
PMCID:
PMC1300175
DOI:
10.1016/S0006-3495(99)77358-3
[Indexed for MEDLINE]
Free PMC Article

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