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Biophys J, July 2000, p. 231-246, Vol. 79, No. 1
Departamento de Bioquímica y Biología Molecular, Facultad de Medicina, C/J Clavería s/n, Universidad de Oviedo, E-33006 Oviedo, Spain
The participation of amino-terminal domains in human
ether-a-go-go
(eag)-related gene (HERG) K+
channel gating was studied using deleted channel variants expressed in
Xenopus oocytes. Selective deletion of the HERG-specific
sequence (HERG 
138-373) located between the conserved initial amino
terminus (the eag or PAS domain) and the first
transmembrane helix accelerates channel activation and shifts its
voltage dependence to hyperpolarized values. However, deactivation time
constants from fully activated states and channel inactivation remain
almost unaltered after the deletion. The deletion effects are equally
manifested in channel variants lacking inactivation. The
characteristics of constructs lacking only about half of the
HERG-specific domain (223-373) or a short stretch of 19 residues
(355-373) suggest that the role of this domain is not related
exclusively to its length, but also to the presence of specific
sequences near the channel core. Deletion-induced effects are partially
reversed by the additional elimination of the eag
domain. Thus the particular combination of HERG-specific and
eag domains determines two important HERG features: the
slow activation essential for neuronal spike-frequency adaptation and
maintenance of the cardiac action potential plateau, and the slow
deactivation contributing to HERG inward rectification.
Biophys J, July 2000, p. 231-246, Vol. 79, No. 1
© 2000 by the Biophysical Society 0006-3495/00/07/231/16 $2.00
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