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Originally published In Press as doi:10.1074/jbc.M005996200 on October 16, 2000

J. Biol. Chem., Vol. 276, Issue 3, 2159-2167, January 19, 2001
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Drosophila melanogaster Casein Kinase II Interacts with and Phosphorylates the Basic Helix-Loop-Helix Proteins m5, m7, and m8 Derived from the Enhancer of split Complex*

Regina L. Trott, Madhavi Kalive, Zeev ParoushDagger , and Ashok P. Bidwai§

From the Department of Biology, West Virginia University, Morgantown, West Virginia 26506-6057 and the Dagger  Department of Biochemistry, The Hebrew University-Hadassah Medical School, Jerusalem 91120, Israel

Drosophila melanogaster casein kinase II (DmCKII) is composed of catalytic (alpha ) and regulatory (beta ) subunits associated as an alpha 2beta 2 heterotetramer. Using the two-hybrid system, we have screened a D. melanogaster embryo cDNA library for proteins that interact with DmCKIIalpha . One of the cDNAs isolated in this screen encodes m7, a basic helix-loop-helix (bHLH)-type transcription factor encoded by the Enhancer of split complex (E(spl)C), which regulates neurogenesis. m7 interacts with DmCKIIalpha but not with DmCKIIbeta , suggesting that this interaction is specific for the catalytic subunit of DmCKII. In addition to m7, we demonstrate that DmCKIIalpha also interacts with two other E(spl)C-derived bHLH proteins, m5 and m8, but not with other members, such as m3 and mC. Consistent with the specificity observed for the interaction of DmCKIIalpha with these bHLH proteins, sequence alignment suggests that only m5, m7, and m8 contain a consensus site for phosphorylation by CKII within a subdomain unique to these three proteins. Accordingly, these three proteins are phosphorylated by DmCKIIalpha , as well as by the alpha 2beta 2 holoenzyme purified from Drosophila embryos. In line with the prediction of a single consensus site for CKII, replacement of Ser159 of m8 with either Ala or Asp abolishes phosphorylation, identifying this residue as the site of phosphorylation. We also demonstrate that m8 forms a direct physical complex with purified DmCKII, corroborating the observed two-hybrid interaction between these proteins. Finally, substitution of Ser159 of m8 with Ala attenuates interaction with DmCKIIalpha , whereas substitution with Asp abolishes the interaction. These studies constitute the first demonstration that DmCKII interacts with and phosphorylates m5, m7, and m8 and suggest a biochemical and/or structural basis for the functional equivalency of these bHLH proteins that is observed in the context of neurogenesis.

* This work was supported by American Cancer Society Grant RPG-9918901-DDC (to A. P. B.) and by grants from the Israel Cancer Research Fund and the Jan M. and Eugenia Krol Charitable Foundation (to Z. P.).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.

§ To whom correspondence should be addressed: Dept. of Biology, P. O. Box 6057, Brooks Hall, West Virginia University, Morgantown, WV 26506-6057. Tel.: 304-293-5201 ext. 2533; Fax: 304-293-6363; E-mail: Abidwai@wvu.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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