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Originally published In Press as doi:10.1074/jbc.M204130200 on May 24, 2002

J. Biol. Chem., Vol. 277, Issue 32, 28545-28553, August 9, 2002
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The Identification and Characterization of a Noncontinuous Calmodulin-binding Site in Noninactivating Voltage-dependent KCNQ Potassium Channels*

Eva Yus-Nájera, Irene Santana-Castro, and Alvaro VillarroelDagger

From the Instituto Cajal, Consejo Superior de Investigaciones, Avenida, Dr. Arce 37, 28002 Madrid, Spain

We show here that in a yeast two-hybrid assay calmodulin (CaM) interacts with the intracellular C-terminal region of several members of the KCNQ family of potassium channels. CaM co-immunoprecipitates with KCNQ2, KCNQ3, or KCNQ5 subunits better in the absence than in the presence of Ca2+. Moreover, in two-hybrid assays where it is possible to detect interactions with apo-CaM but not with Ca2+-bound calmodulin, we localized the CaM-binding site to a region that is predicted to contain two alpha -helices (A and B). These two helices encompass ~85 amino acids, and in KCNQ2 they are separated by a dispensable stretch of ~130 amino acids. Within this CaM-binding domain, we found an IQ-like CaM-binding motif in helix A and two overlapping consensus 1-5-10 CaM-binding motifs in helix B. Point mutations in helix A or B were capable of abolishing CaM binding in the two-hybrid assay. Moreover, glutathione S-transferase fusion proteins containing helices A and B were capable of binding to CaM, indicating that the interaction with KCNQ channels is direct. Full-length CaM (both N and C lobes) and a functional EF-1 hand were required for these interactions to occur. These observations suggest that apo-CaM is bound to neuronal KCNQ channels at low resting Ca2+ levels and that this interaction is disturbed when the [Ca2+] is raised. Thus, we propose that CaM acts as a mediator in the Ca2+-dependent modulation of KCNQ channels.

* This work was supported by European Union Grant QLGT-1999-00827, Fondo de Investigaciones Sanitarias Grant FIS01/1136), Comunidad de Madrid Grant 08.5/0011/2001.1, and Spanish Ministry of Education Grant SAF2000-0159).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed. Tel.: 34-91-585-4718; Fax: 34-91-585-4754; E-mail: av@cajal.csic.es.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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