Lilliana Radoshevich

Dr. Radoshevich completed her Ph.D at the University of California, San Francisco. There her work in the Debnath laboratory identified a novel substrate of the ubiquitin-like protein, ATG12 and demonstrated that the ATG12-ATG3 complex alters mitochondrial morphology. As a post-doctoral researcher under Pascale Cossart at the Institut Pasteur, she identified an early Interferon-independent induction of the ubiquitin-like protein ISG15. Her research also established that ISG15 could act as antibacterial effector following Listeria monocytogenes infection through a conjugation-dependent mechanism that correlates with increased cytokine secretion. Presently, at the University of Iowa she directs her own laboratory that uses cutting edge proteomics to study the effect of intracellular bacterial pathogens on ubiquitin-like proteins. Ubiquitin-like modifications (UBLs) are rapid, reversible and can profoundly alter cell fate and function. Intriguingly, the majority of UBLs are involved in the cellular response to stress, in particular the response to infection, ER-stress and autophagy. The laboratory aims to address the fundamental question of how the cell responds to stress by decoding novel networks of covalent protein complexes. To do so, they compare infection with two intracellular pathogens: Listeria monocytogenes and Francisella novicida which both secrete virulence factors known to hijack and thwart cellular stress responses in order to unravel novel mechanisms of ubiquitin and UBL function.