Protease inhibitors and proteolytic signalling cascades in insects |
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Authors: | David Gubb Arantza Sanz-Parra Laura Barcena Laurent Troxler Ane Fullaondo |
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Affiliation: | 1. Department of Functional Genomics, CICbioGUNE Institute, Bizkaia Technology Park, Ed. 801A, 48160 Derio, Spain;2. IBMC, UPR 9022 du CNRS, 15 rue Rene Descartes, F67084 Strasbourg Cedex, France |
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Abstract: | Proteolytic signalling cascades control a wide range of physiological responses. In order to respond rapidly, protease activity must be maintained at a basal level: the component zymogens must be sequentially activated and actively degraded. At the same time, signalling cascades must respond precisely: high target specificity is required. The insects have a wide range of trapping- and tight-binding protease inhibitors, which can regulate the activity of individual proteases. In addition, the interactions between component proteases of a signalling cascade can be modified by serine protease homologues. The suicide-inhibition mechanism of serpin family inhibitors gives rapid turnover of both protease and inhibitor, but target specificity is inherently broad. Similarly, the TEP/macroglobulins have extremely broad target specificity, which suits them for roles as hormone transport proteins and sensors of pathogenic virulence factors. The tight-binding inhibitors, on the other hand, have a lock-and-key mechanism capable of high target specificity. In addition, proteins containing multiple tight-binding inhibitory domains may act as scaffolds for the assembly of signalling complexes. Proteolytic cascades regulated by combinations of different types of inhibitor could combine the rapidity of suicide-inhibitors with the specificity lock-and-key inhibitors. This would allow precise control of physiological responses and may turn out to be a general rule. |
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Keywords: | Insect Protease inhibitors Serpin Kazal Signalling |
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