@article {836191,
	title = {Rasp, a putative transmembrane acyltransferase, is required for Hedgehog signaling.},
	journal = {Development},
	volume = {129},
	number = {4},
	year = {2002},
	month = {2002 Feb},
	pages = {843-51},
	abstract = {
	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.

},
	keywords = {Acyltransferases, Amino Acid Sequence, Animals, Drosophila melanogaster, Drosophila Proteins, Hedgehog Proteins, Membrane Proteins, Molecular Sequence Data, Phenotype, Proto-Oncogene Proteins, Signal Transduction, Transcriptional Activation, Wnt1 Protein},
	issn = {0950-1991},
	author = {Micchelli, Craig A and The, Inge and Selva, Erica and Mogila, Vladic and Perrimon, Norbert}
}
