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Biophysical Journal 66: 667-673 (1994)
© 1994 the Biophysical Society

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Structural determinant for assembly of mammalian K+ channels.

T E Lee, L H Philipson, A Kuznetsov and D J Nelson

University of Chicago, Department of Neurology, Illinois 60637.

ABSTRACT

K+ channel function is regulated through the assembly of channel subunit isoforms into either homo- or heterotetrameric structures each characterized by distinct pharmacologic and kinetic properties. In studying the molecular basis of subunit association in mammalian Shaker-like K+ channels, we constructed deletion mutants of the inactivating K+ channel hKv1.4 alone and in tandem with hKv1.5 and examined the functional properties electrophysiologically in Xenopus oocytes. Deletion of 255 amino acids in the amino-terminal domain of hKv1.4 prevented the formation of hybrid channels within the subfamily but had no effect on homomultimerization or voltage-dependent gating. The amino-terminal deletion mutant of Kv2.1, a noninactivating K+ channel from a distantly related subfamily also forms functional homomultimeric channels. Although members of different K+ channel subfamilies do not coassemble, coexpression of the amino-terminal deletion mutants of hKv1.4 and Kv2.1 resulted in the formation of functional hybrid channels. These results demonstrate that the amino-terminal region of mammalian K+ channels subserves two functions. It provides a recognition site necessary for hetero- but not homomultimeric channel assembly within a subfamily and prevents coassembly between subfamilies.




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A. Kosolapov and C. Deutsch
Folding of the Voltage-gated K+ Channel T1 Recognition Domain
J. Biol. Chem., January 31, 2003; 278(6): 4305 - 4313.
[Abstract] [Full Text] [PDF]


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Copyright © 1994 by the Biophysical Society.