[No authors listed]
The mammalian cis-trans prolyl isomerase Pin1 and its yeast orthologue Ess1/Ptf1 have been implicated in cell cycle control but a correlation between biochemical and physiological functions has not been established conclusively. Pin1 targets the proline residue carboxy-terminal to the phosphorylated threonine or serine residue, which constitutes part of the phosphorylated mitogen-activated protein kinase (MAPK) site PXpT/SP. Here we show that the Drosophila Pin1 homologue, the Dodo protein, is involved in dorsoventral patterning of the follicular epithelium in the egg chamber. Its function is to facilitate the degradation of transcription factor CF2, which requires, a priori, activated epidermal growth factor receptor-MAPK signalling.
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