Calmodulin defects cause the loss of Ca2(+)-dependent K+ currents in two pantophobiac mutants of Paramecium tetraurelia.

Two behavioral mutants of Paramecium tetraurelia, pantophobiacs A1 and A2, have single amino acid defects in the structure of calmodulin. The mutants exhibit several major ion current defects under voltage clamp: (i) the Ca2(+)-dependent K+ current activated upon depolarization of Paramecium is greatly reduced or missing in both mutants, (ii) both mutants lack a Ca2(+)-dependent K+ current activated upon hyperpolarization, and (iii) the Ca2(+)-dependent Na+ current is significantly smaller in pantophobiac A1 compared with the wild type, whereas this current is slightly increased in pantophobiac A2. Other, minor defects include a reduction in peak amplitude of the depolarization-activated Ca2+ current in pantophobiac A2, increased rates of voltage-dependent inactivation of this Ca2+ current in both pantophobiac A1 and pantophobiac A2, and an increase in the time required for the hyperpolarization-activated Ca2+ current to recover from inactivation in the pantophobiacs. The diversity of the pantophobiac mutations' effects on ion current function may indicate specific associations of calmodulin with a variety of Ca2(+)-related ion channel species in Paramecium.