@article {5596,
	title = {The full-length unprocessed hedgehog protein is an active signaling molecule.},
	journal = {The Journal of biological chemistry},
	volume = {285},
	number = {4},
	year = {2010},
	note = {n/a
},
	month = {2010 Jan 22},
	pages = {2562-8},
	abstract = {The hedgehog (HH) family of ligands plays an important instructional role in metazoan development. HH proteins are initially produced as approximately 45-kDa full-length proteins, which undergo an intramolecular cleavage to generate an amino-terminal product that subsequently becomes cholesterol-modified (HH-Np). It is well accepted that this cholesterol-modified amino-terminal cleavage product is responsible for all HH-dependent signaling events. Contrary to this model we show here that full-length forms of HH proteins are able to traffic to the plasma membrane and participate directly in cell-cell signaling, both in vitro and in vivo. We were also able to rescue a Drosophila eye-specific hh loss of function phenotype by expressing a full-length form of hh that cannot be processed into HH-Np. These results suggest that in some physiological contexts full-length HH proteins may participate directly in HH signaling and that this novel activity of full-length HH may be evolutionarily conserved.
},
	author = {Tokhunts, Robert and Singh, Samer and Chu, Tehyen and D{\textquoteright}Angelo, Gisela and Baubet, Valerie and Goetz, John A and Huang, Zhen and Yuan, Ziqiang and Ascano, Manuel and Zavros, Yana and Th{\'e}rond, Pascal P and Kunes, Sam and Dahmane, Nadia and Robbins, David J}
}
