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Originally published In Press as doi:10.1074/jbc.M211907200 on January 15, 2003

J. Biol. Chem., Vol. 278, Issue 12, 10073-10080, March 21, 2003
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Monomeric 14-3-3 Protein Is Sufficient to Modulate the Activity of the Drosophila Slowpoke Calcium-dependent Potassium Channel*

Yi ZhouDagger §, Smitha ReddyDagger , Heather Murrey, Hong Fei, and Irwin B. Levitan

From the Department of Neuroscience, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104

Drosophila 14-3-3zeta (D14-3-3zeta ) modulates the activity of the Slowpoke calcium-dependent potassium channel (dSlo) by interacting with the dSlo binding protein, Slob. We show here that D14-3-3zeta forms dimers in vitro. Site-directed mutations in its putative dimerization interface result in a dimerization-deficient form of D14-3-3zeta . Both the wild-type and dimerization-deficient forms of D14-3-3zeta bind to Slob with similar affinity and form complexes with dSlo. When dSlo and Slob are expressed in mammalian cells, the dSlo channel activity is similarly modulated by co-expression of either the wild-type or the dimerization-deficient form of D14-3-3zeta . In addition, dSlo is still modulated by wild-type D14-3-3zeta in the presence of a 14-3-3 mutant, which does not itself bind to Slob but forms heterodimers with the wild-type 14-3-3. These data, taken together, suggest that monomeric D14-3-3zeta is capable of modulating dSlo channel activity in this regulatory complex.

* This work was supported by a grant from the National Institutes of Health (to I. B. L.).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 Both authors contributed equally to this work.

§ To whom correspondence should be addressed. Tel.: 215-898-2122; Fax: 215-573-2015; E-mail: yizhou@mail.med.upenn.edu.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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