Journal
CLINICAL & TRANSLATIONAL IMMUNOLOGY
Volume 8, Issue 8, Pages -Publisher
WILEY
DOI: 10.1002/cti2.1073
Keywords
bacterial toxins; cancer; furin; guanylate-binding proteins; proprotein convertases; viral glycoproteins
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Funding
- DFG [SPP 1923]
- International Graduate School in Molecular Medicine Ulm (IGradU)
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Proteolytic cleavage regulates numerous processes in health and disease. One key player is the ubiquitously expressed serine protease furin, which cleaves a plethora of proteins at polybasic recognition motifs. Mammalian substrates of furin include cytokines, hormones, growth factors and receptors. Thus, it is not surprising that aberrant furin activity is associated with a variety of disorders including cancer. Furthermore, the enzymatic activity of furin is exploited by numerous viral and bacterial pathogens, thereby enhancing their virulence and spread. In this review, we describe the physiological and pathophysiological substrates of furin and discuss how dysregulation of a simple proteolytic cleavage event may promote infectious diseases and cancer. One major focus is the role of furin in viral glycoprotein maturation and pathogenicity. We also outline cellular mechanisms regulating the expression and activation of furin and summarise current approaches that target this protease for therapeutic intervention.
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