PMID:8689684

Citation	Porter, JA, Ekker, SC, Park, WJ, von Kessler, DP, Young, KE, Chen, CH, Ma, Y, Woods, AS, Cotter, RJ, Koonin, EV and Beachy, PA (1996) Hedgehog patterning activity: role of a lipophilic modification mediated by the carboxy-terminal autoprocessing domain. Cell 86:21-34
Abstract	Autocatalytic processing mediated by the carboxyterminal domain of the hedgehog (hh) protein precursor (Hh) generates an amino-terminal product that accounts for all known signaling activity. The role of autoprocessing biogenesis of the hh signal has been unclear, since a truncated unprocessed protein lacking all carboxy-terminal domain sequences retains signaling activity. Here, we present evidence that the autoprocessing reaction proceeds via an internal thioester intermediate and results in a covalent modification that increases the hydrophobic character of the signaling domain and influences its spatial and subcellular distribution. We demonstrate that truncated unprocessed amino-terminal protein causes embryonic mispatterning, even when expression is localized to cells that normally express Hh, thus suggesting a role for autoprocessing in spatial regulation of hh signaling. This type of processing also appears to operate in the biogenesis of other novel secreted proteins.
Links	PubMed
Keywords	Animals; Cells, Cultured/physiology; Consensus Sequence; Drosophila/embryology; Drosophila Proteins; Esters/chemistry; Hedgehog Proteins; Lipids/chemistry; Mass Spectrometry; Molecular Sequence Data; Protein Structure, Tertiary; Proteins/chemistry; Proteins/genetics; Sequence Homology, Amino Acid; Signal Transduction/physiology; Sulfhydryl Compounds/chemistry; Water/chemistry
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