Tip of another iceberg: Drosophila serpins.
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.
Reichhart
Jean-Marc
JM
Institut de Biologie Moléculaire et Cellulaire, UPR 9022 du CNRS, 15 rue Rene Descartes, F67084 Strasbourg Cedex, France. JM.Reichhart@ibmc.u-strasbg.fr
D000818:Animals; D029721:Drosophila Proteins / Q000737:chemistry / Q000502:physiology*; D004331:Drosophila melanogaster / Q000196:embryology / Q000235:genetics / Q000502:physiology*; D007109:Immunity; D011487:Protein Conformation; D015842:Serine Proteinase Inhibitors / Q000737:chemistry / Q000502:physiology; D015843:Serpins / Q000737:chemistry / Q000502:physiology*
D029721:Drosophila Proteins; D015842:Serine Proteinase Inhibitors; D015843:Serpins; C468118:Spn27A protein, Drosophila; C417282:nec protein, Drosophila