Drosophila Cdi4 is a p21/p27/p57-like cyclin-dependent kinase inhibitor with specificity for cyclin E complexes.

This paper describes the use of a yeast two-hybrid interaction mating assay to screen large panels of proteins for informative interactions. In one of our first panel screens we discovered that Drosophila cyclin E interacts with two other Drosophila proteins, Rux and Cdi4. This finding led to new hypotheses about the function of Rux and Cdi4.

While we were characterizing Cdi4 and its interaction with cyclin E, two groups, one led by de Nooij and Hariharan and the other by Lane and Lehner, independently isolated mutations in a gene, decapo, that encodes Cdi4. Both groups presented elegant experiments demonstrating the importance of decapo in regulating the cell cycle during development (de Nooij et al., 1996. Cell 87, 1237-1247 [Medline]; Lane et al., 1997. Cell 87, 1225-1235 [Medline]). Our paper includes some data not duplicated by the work from de Nooij et al., or Lane et al., including in vitro kinase inhibition assays, yeast interaction assays, and our sequence analyses. This paper is not published. To reference data in this paper please refer to R.L. Finley, B. Cohen, an R. Brent, personal communication, or refer to this web site.

Thomas and Zipursky and colleagues have studied the function of Rux, a negative regulator of the cell cycle in the developing eye. The function of Rux and its interaction with cyclins was further explored, and a model for how Rux works was published by Thomas et al. 1997, Genes & Development, 11:94-105 [Medline].

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