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  • Title: Regulation of adenylyl cyclase from Paramecium by an intrinsic potassium conductance.
    Author: Schultz JE, Klumpp S, Benz R, Schürhoff-Goeters WJ, Schmid A.
    Journal: Science; 1992 Jan 31; 255(5044):600-3. PubMed ID: 1371017.
    Abstract:
    Hyperpolarization of the cell membrane of Paramecium stimulates adenosine 3',5'-monophosphate (cAMP) formation. Manipulations of the K+ resting conductance of the ciliate by adaptation in different buffers affected excitability of the cAMP generating system. Blockade of K+ channels inhibited hyperpolarization-stimulated cAMP formation. A mutant of Paramecium that is unable to control its K+ resting conductance had a defect in cAMP formation. Purified adenylyl cyclase, when incorporated into an artificial lipid bilayer membrane, revealed properties of a voltage-independent K+ channel. This indicates that the adenylyl cyclase of Paramecium has a secondary function as carrier of the K+ resting conductance. A hyperpolarization-activated K+ efflux appears to directly regulate adenylyl cyclase activity in vivo.
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