MinK Potassium Channels Are Heteromultimeric Complexes

• Published in: The Journal of biological chemistry Vol. 272; no. 3; pp. 1654 - 1658
• Main Authors: Tai, Kwok-Keung, Wang, Ke-Wei, Goldstein, Steve A.N.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 17.01.1997; American Society for Biochemistry and Molecular Biology
• Subjects: Animals; Cysteine - analysis; Ethyl Methanesulfonate - analogs & derivatives; Ethyl Methanesulfonate - pharmacology; Potassium Channel Blockers; Potassium Channels - chemistry; Potassium Channels, Voltage-Gated; Rats; Recombinant Proteins - antagonists & inhibitors; Recombinant Proteins - chemistry; Tetraethylammonium; Tetraethylammonium Compounds - pharmacology; Xenopus laevis
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1074/jbc.272.3.1654

MinK is a transmembrane protein of 130 amino acids found in the kidney, heart, and vestibular system of mammals. Its expression in Xenopus laevis oocytes induces a voltage-dependent potassium current similar to that seen in vivo. Indirect evidence has fueled speculation that function requires association of MinK and another protein endogenous to oocytes and native tissues. In this report, we show that direct covalent modification of an oocyte membrane protein alters properties of the MinK ion conduction pore; modified channels exhibit decreased potassium conduction and increased permeability to sodium and cesium. The modifying reagents, two membrane-impermeant, sulfhydryl-specific methanethiosulfonate derivatives, react only from the extracellular solution at rates that are determined by the conformational state of the channel. These findings indicate that MinK is intimately associated with an oocyte protein whose exposure to the external solution changes during channel gating and which acts with MinK to establish ion conduction pore function.