New lives for old: evolution of pseudoenzyme function illustrated by iRhoms
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Molecular Biology
Link
http://www.nature.com/articles/nrm3392.pdf
Reference87 articles.
1. Todd, A., Orengo, C. & Thornton, J. Sequence and structural differences between enzyme and nonenzyme homologs. Structure 10, 1435–1451 (2002). A comprehensive and pioneering comparison of enzymes and their catalytically inactive cognates, incorporating sequence, structural and functional analysis. Highlights the process of dead enzyme evolution.
2. Puente, X., Sanchez, L., Overall, C. & Lopez-Otin, C. Human and mouse proteases: a comparative genomic approach. Nature Rev. Genet. 4, 544–558 (2003).
3. Pils, B. & Schultz, J. Inactive enzyme-homologues find new function in regulatory processes. J. Mol. Biol. 340, 399–404 (2004). Large scale analysis of inactive enzyme homologues that emphasizes the prevalence of inactive cognates and their conservation in metazoans. It also proposes that dead enzymes frequently acquire regulatory functions.
4. Zettl, M., Adrain, C., Strisovsky, K., Lastun, V. & Freeman, M. Rhomboid family pseudoproteases use the ER quality control machinery to regulate intercellular signaling. Cell 145, 79–91 (2011). Shows that iRhoms are catalytically inactive rhomboid protease homologues, and that in D. melanogaster they inhibit EGFR signalling by binding EGF ligands and directing them into ERAD.
5. Adrain, C., Zettl, M., Christova, Y., Taylor, N. & Freeman, M. Tumor necrosis factor signaling requires iRhom2 to promote trafficking and activation of TACE. Science 335, 225–228 (2012).
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