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Papers In Press, published online ahead of print May 24, 2002
J. Biol. Chem, 10.1074/jbc.M204130200
Submitted on April 29, 2002
Revised on May 22, 2002
Accepted on May 24, 2002

The identification and characterization of a non-continuous calmodulin binding site in non-inactivating voltage-dependent KCNQ potassium channels

Eva Yus-Najera, Irene Santana-Castro, and Alvaro Villarroel

Plasticidad Neural, Instituto Cajal - CSIC, Madrid 28002

Corresponding Author: av{at}cajal.csic.es

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+-CaM, we localized the CaM binding site to a region that is predicted to contain two a-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, GST fusion proteins containing helices A-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.


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