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rasp, a putative transmembrane acyltransferase, is required for Hedgehog signaling

Craig A. Micchelli^1,2,*, Inge The^1,, Erica Selva¹, Vladic Mogila¹ and Norbert Perrimon^1,2

¹ Department of Genetics, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA
² Howard Hughes Medical Institute, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA
Present address: Department of Molecular Medicine, NRB Floor 6, Office 621, 364 Plantation Street, Worcester, MA 01615, USA

*Author for correspondence (e-mail: cmicchel{at}genetics.med.harvard.edu)

Accepted 6 November 2001

Members of the Hedgehog (Hh) family encode secreted molecules that act as potent organizers during vertebrate and invertebrate development. Post-translational modification regulates both the range and efficacy of Hh protein. One such modification is the acylation of the N-terminal cysteine of Hh. In a screen for zygotic lethal mutations associated with maternal effects, we have identified rasp, a novel Drosophila segment polarity gene. Analysis of the rasp mutant phenotype, in both the embryo and wing imaginal disc demonstrates that rasp does not disrupt Wnt/Wingless signaling but is specifically required for Hh signaling. The requirement of rasp is restricted only to those cells that produce Hh; hh transcription, protein levels and distribution are not affected by the loss of rasp. Molecular analysis reveals that rasp encodes a multipass transmembrane protein that has homology to a family of membrane bound O-acyl transferases. Our results suggest that Rasp-dependent acylation is necessary to generate a fully active Hh protein.

Key words: rasp, hedgehog, Acyltransferase, Wing imaginal disc, Drosophila

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