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Papers In Press, published online ahead of print February 16, 2003
Department of Physiology II, University of Freiburg, Freiburg 79104
Corresponding Author: bernd.fakler{at}physiologie.uni-freiburg.de
Cumulative inactivation of voltage-gated (Kv) K+ channels shapes the presynaptic action potential and determines timing and strength of synaptic transmission. Kv1.4 channels exhibit rapid ‘ball-and-chain’-type inactivation gating; different from all other Kva subunits, Kv1.4 harbors two inactivation domains at its N-terminus. Here we report the solution structure and function of this 'tandem-inactivation domain' using NMR spectroscopy and patch-clamp recordings. Inactivation domain 1 (ID1, residues 1-38) consists of a flexible N-terminus anchored at a 5-turn helix, while ID2 (residues 40-50) is a 2.5-turn helix made up of small hydrophobic amino acids. Functional analysis suggests that only ID1 may work as a pore-occluding ball domain, while ID2 most likely acts as a 'docking domain' that attaches ID1 to the cytoplasmic face of the channel. Deletion of ID2 slows inactivation considerably and largely impairs cumulative inactivation. Together, the concerted action of ID1 and ID2 may promote rapid inactivation of Kv1.4 that is crucial for the channel's function in short-term plasticity.
J. Biol. Chem, 10.1074/jbc.M210191200
Submitted on October 4, 2002
Revised on February 14, 2003
Accepted on February 16, 2003
Solution structure and function of the 'tandem-inactivation domain' of the neuronal A-type potassium channel Kv1.4
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