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First published online 15 March 2006
doi: 10.1242/dev.02334

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smoothened and thickveins regulate Moleskin/Importin 7-mediated MAP kinase signaling in the developing Drosophila eye

Alysia D. Vrailas¹, Daniel R. Marenda¹, Summer E. Cook¹, Maureen A. Powers¹, James A. Lorenzen^2,3, Lizabeth A. Perkins² and Kevin Moses^1,*,

¹ Department of Cell Biology, Emory University School of Medicine, Atlanta, GA 30322, USA.
² Pediatric Surgical Research Laboratories, Massachusetts General Hospital, Harvard Medical School Boston, MA 02114, USA.
³ Department of Pediatric Gastroenterology, Medical College of Wisconsin, Milwaukee, WI 53226, USA.

Author for correspondence (e-mail: mosesk{at}hhmi.org)

Accepted 17 February 2006

The Drosophila Mitogen Activated Protein Kinase (MAPK) Rolled is a key regulator of developmental signaling, relaying information from the cytoplasm into the nucleus. Cytoplasmic MEK phosphorylates MAPK (pMAPK), which then dimerizes and translocates to the nucleus where it regulates transcription factors. In cell culture, MAPK nuclear translocation directly follows phosphorylation, but in developing tissues pMAPK can be held in the cytoplasm for extended periods (hours). Here, we show that Moleskin antigen (Drosophila Importin 7/Msk), a MAPK transport factor, is sequestered apically at a time when lateral inhibition is required for patterning in the developing eye. We suggest that this apical restriction of Msk limits MAPK nuclear translocation and blocks Ras pathway nuclear signaling. Ectopic expression of Msk overcomes this block and disrupts patterning. Additionally, the MAPK cytoplasmic hold is genetically dependent on the presence of Decapentaplegic (Dpp) and Hedgehog receptors.

Key words: Drosophila, moleskin, Importin 7, Morphogenetic furrow, MAP kinase, Cell cycle, Nuclear translocation, ERK, Hedgehog, Dpp, Egfr

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