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J. Biol. Chem., Vol. 283, Issue 37, 25105-25109, September 12, 2008

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Minireview

Tethering Chemistry and K⁺ Channels^*

From the Department of Biochemistry and Molecular Pharmacology, Programs in Neuroscience and Chemical Biology, University of Massachusetts Medical School, Worcester, Massachusetts 01605-2324

Voltage-gated K⁺ channels are dynamic macromolecular machines that open and close in response to changes in membrane potential. These multisubunit membrane-embedded proteins are responsible for governing neuronal excitability, maintaining cardiac rhythmicity, and regulating epithelial electrolyte homeostasis. High resolution crystal structures have provided snapshots of K⁺ channels caught in different states with incriminating molecular detail. Nonetheless, the connection between these static images and the specific trajectories of K⁺ channel movements is still being resolved by biochemical experimentation. Electrophysiological recordings in the presence of chemical modifying reagents have been a staple in ion channel structure/function studies during both the pre- and post-crystal structure eras. Small molecule tethering agents (chemoselective electrophiles linked to ligands) have proven to be particularly useful tools for defining the architecture and motions of K⁺ channels. This Minireview examines the synthesis and utilization of chemical tethering agents to probe and manipulate the assembly, structure, function, and molecular movements of voltage-gated K⁺ channel protein complexes.

^* This work was supported, in whole or in part, by National Institutes of Health Grants GM-070650 and DC-007669. This minireview will be reprinted in the 2008 Minireview Compendium, which will be available in January, 2009.

¹ To whom correspondence should be addressed. E-mail: william.kobertz{at}umassmed.edu.

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