Abstract
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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Acknowledgements
We thank D. Spyropoulos, M. Trojanowska and D. Watson for valuable comments on the manuscript; N. Perrimon for providing the hs-D-rafgof flies; G.L.G. Miklos for the gift of the flightless-I transgenic stocks; and X. Zhang of the Medical University of South Carolina Antibody Production Facility for producing antisera. This work is supported by a grant from the National Institutes of Health to T.H. and a grant from the American Heart Association to H.G.d.G.
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Hsu, T., McRackan, D., Vincent, T. et al. Drosophila Pin1 prolyl isomerase Dodo is a MAP kinase signal responder during oogenesis. Nat Cell Biol 3, 538–543 (2001). https://doi.org/10.1038/35078508
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DOI: https://doi.org/10.1038/35078508
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