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Science 2 December 1994:
Vol. 266. no. 5190, pp. 1528 - 1537
DOI: 10.1126/science.7985023

Articles

Science, Vol 266, Issue 5190, 1528-1537
Copyright © 1994 by American Association for the Advancement of Science


articles

Autoproteolysis in hedgehog protein biogenesis

JJ Lee, SC Ekker, DP von Kessler, JA Porter, BI Sun, and PA Beachy

Howard Hughes Medical Institute, Department of Molecular Biology and Genetics, Johns Hopkins School of Medicine, Baltimore, MD 21205.

Extracellular signaling proteins encoded by the hedgehog (hh) multigene family are responsible for the patterning of a variety of embryonic structures in vertebrates and invertebrates. The Drosophila hh gene has now been shown to generate two predominant protein species that are derived by an internal autoproteolytic cleavage of a larger precursor. Mutations that reduced the efficiency of autoproteolysis in vitro diminished precursor cleavage in vivo and also impaired the signaling and patterning activities of the HH protein. The two HH protein species exhibited distinctive biochemical properties and tissue distribution, and these differences suggest a mechanism that could account for the long- and short-range signaling activities of HH in vivo.


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Skinny Hedgehog, an Acyltransferase Required for Palmitoylation and Activity of the Hedgehog Signal.
Z. Chamoun, R. K. Mann, D. Nellen, D. P. von Kessler, M. Bellotto, P. A. Beachy, and K. Basler (2001)
Science 293, 2080-2084
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Science. ISSN 0036-8075 (print), 1095-9203 (online)