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Revisiting Bacterial Ubiquitin Ligase Effectors: Weapons for Host Exploitation

1
Department of Experimental and Clinical Medicine, University “Magna Graecia” of Catanzaro, 88100 Catanzaro, Italy
2
Department of Molecular Medicine and Medical Biotechnologies, University of Naples “Federico II”, 80131 Naples, Italy
*
Authors to whom correspondence should be addressed.
Giuseppe Fiume and Ileana Quinto should be considered as co-last authors.
Int. J. Mol. Sci. 2018, 19(11), 3576; https://doi.org/10.3390/ijms19113576
Received: 17 October 2018 / Revised: 31 October 2018 / Accepted: 8 November 2018 / Published: 13 November 2018
(This article belongs to the Special Issue The Ubiquitin Code in Cellular Signaling and Homeostasis)
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Abstract

Protein ubiquitylation plays a central role in eukaryotic cell physiology. It is involved in several regulatory processes, ranging from protein folding or degradation, subcellular localization of proteins, vesicular trafficking and endocytosis to DNA repair, cell cycle, innate immunity, autophagy, and apoptosis. As such, it is reasonable that pathogens have developed a way to exploit such a crucial system to enhance their virulence against the host. Hence, bacteria have evolved a wide range of effectors capable of mimicking the main players of the eukaryotic ubiquitin system, in particular ubiquitin ligases, by interfering with host physiology. Here, we give an overview of this topic and, in particular, we detail and discuss the mechanisms developed by pathogenic bacteria to hijack the host ubiquitination system for their own benefit. View Full-Text
Keywords: ubiquitin ligase; T3SS; T4SS ubiquitin ligase; T3SS; T4SS
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).
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Pisano, A.; Albano, F.; Vecchio, E.; Renna, M.; Scala, G.; Quinto, I.; Fiume, G. Revisiting Bacterial Ubiquitin Ligase Effectors: Weapons for Host Exploitation. Int. J. Mol. Sci. 2018, 19, 3576.

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