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Updated: Apr 23, 2026

In-vitro Reconstitution of Bacterial Ubiquitination and VCP/p97-mediated Elimination
Published on: January 2, 2026
Bacterial effectors and their functions in the ubiquitin-proteasome system: insight from the modes of substrate
Minsoo Kim1, Ryota Otsubo2, Hanako Morikawa3
1Division of Bacterial Infection Biology, Institute of Medical Science, The University of Tokyo, Shirokanedai 4-6-1, Minato-ku 4-6-1, Tokyo 108-8639, Japan. minsoo@ims.u-tokyo.ac.jp.
Abstract:
Protein ubiquitination plays indispensable roles in the regulation of cell homeostasis and pathogenesis of neoplastic, infectious, and neurodegenerative diseases. Given the importance of this modification, it is to be expected that several pathogenic bacteria have developed the ability to utilize the host ubiquitin system for their own benefit. Modulation of the host ubiquitin system by bacterial effector proteins inhibits innate immune responses and hijacks central signaling pathways. Bacterial effectors mimic enzymes of the host ubiquitin system, but may or may not be structurally similar to the mammalian enzymes. Other effectors bind and modify components of the host ubiquitin system, and some are themselves subject to ubiquitination. This review will describe recent findings, based on structural analyses, regarding how pathogens use post-translational modifications of proteins to establish an infection.
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