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Trends Cell Biol. 2005 Dec;15(12):659-65. Epub 2005 Nov 2.

Tip of another iceberg: Drosophila serpins.

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Institut de Biologie Mol├ęculaire et Cellulaire, UPR 9022 du CNRS, 15 rue Rene Descartes, F67084 Strasbourg Cedex, France.


Serpins are serine protease inhibitors with a conserved structure that have been identified in nearly all species and act as suicide substrates by binding covalently to their target proteases. Serpins regulate various physiological processes and defence mechanisms. In humans, several serpin mutations are linked to diseases. The genome of Drosophila melanogaster encodes 29 serpins and even more serine proteases. To date, three serpins have been investigated in detail. Spn27A controls the Toll pathway during early development and is involved in defence reactions in adult flies. SPN42DaA is an inhibitor of furin, a subtilisin-like convertase that is required for pro-protein maturation. Spn43Ac controls the Toll pathway during the immune response. In each case, Drosophila genetics has shed new light on the function of these serine protease inhibitors.

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