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Journal of Neuroscience, Vol 14, 1385-1393, Copyright © 1994 by Society for Neuroscience
Both N- and C-terminal regions contribute to the assembly and functional expression of homo- and heteromultimeric voltage-gated K+ channels
WF Hopkins, V Demas and BL Tempel
Geriatric Research Education and Clinical Center, Veterans Affairs Medical Center, Seattle, Washington 98108.
The functional diversity of voltage-gated K+ channels may be partially
determined by the mechanisms that permit or limit the assembly of
molecularly diverse K+ channel subunits. To determine possible amino acid
sequence domains required for subunit assembly and expression, we have
constructed 15 N- and C-terminal interstitial or truncation deletion
mutations in mKv1.1 (MBK1), a mouse Shaker-like K+ channel. We injected
Xenopus oocytes with cRNA encoding each of these mutants and coinjected
each mutant cRNA with cRNA for wild-type mKv1.3, another mouse Shaker-like
K+ channel that can form heteromultimers with mKv1.1. We found that the
last five amino acids of the C-terminus of mKv1.1 contribute to functional
expression by (1) rescuing the function of mutants with a large truncation
of the C-terminus (delta 424-495), and (2) contributing to the slow
inactivation kinetics (time constant of 2- 3 sec) of wild-type mKv1.1
whole-cell K+ currents. All C-terminal deletion mutants were able to
express at least as heteromultimers with mKv1.3, suggesting that the
C-terminus is not required for channel assembly. In contrast, nine
different interstitial or truncation mutants in which part of a highly
conserved, large (80-99 amino acid residues) domain within the N-terminus
had been deleted were unable to express either homomultimers or
heteromultimers. The relatively small sizes and nonoverlapping
distributions of the interstitial deletions enable us to suggest that the
structural integrity of this entire N- terminal domain is required for
subunit assembly and functional expression of this and probably other
Shaker-like K+ channel proteins.
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