作者: Mariola J. Edelmann , Holger B. Kramer , Mikael Altun , Benedikt M. Kessler
DOI: 10.1111/J.1742-4658.2010.07665.X
关键词:
摘要: Microbial pathogens exploit the ubiquitin system to facilitate infection and manipulate immune responses of host. In this study, susceptibility Yersinia enterocolitica pseudotuberculosis invasion was found be increased upon overexpression deubiquitinating enzyme otubain 1 (OTUB1), a member ovarian tumour domain-containing protein family. Conversely, OTUB1 knockdown interfered with in HEK293T cells as well primary monocytes. This effect attributed modulation bacterial uptake. We demonstrate that Yersinia-encoded virulence factor YpkA (YopO) kinase interacts post-translationally modified form contains multiple phosphorylation sites. OTUB1, small GTPase ras homologue gene family A (RhoA) were part same complex, suggesting RhoA levels are modulated by OTUB1. Our results show is able stabilize active prior invasion, which concomitant an increase post-translational modifications new entry point for manipulating interactions