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,
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