Ubiquitin-regulating effector proteins from Legionella

Ubiquitin is relatively modest in size but involves almost entire cellular signaling pathways. The primary role of ubiquitin is maintaining cellular protein homeostasis. Ubiquitination regulates the fate of target proteins using the proteasome-or autophagy-mediated degradation of ubiquitinated substrates, which can be either intracellular or foreign proteins from invading pathogens. Legionella, a gram-negative intracellular pathogen, hinders the host-ubiquitin system by translocating hundreds of effector pro-teins into the host cell???s cytoplasm. In this review, we describe the current understanding of ubiquitin machinery from Legionella. We summarize structural and biochemical differences between the host-ubiquitin system and ubiquitin-related effectors of Legio-nella. Some of these effectors act much like canonical host-ubi-quitin machinery, whereas others have distinctive structures and accomplish non-canonical ubiquitination via novel biochemical mechanisms. [BMB Reports 2022; 55(7): 316-322]

Automated summary

Ubiquitin, a small molecule, plays an important role in cellular signaling pathways and maintaining protein homeostasis. Legionella, a gram-negative intracellular pathogen, disrupts the host-ubiquitin system by translocating effector proteins into the host cell's cytoplasm. This review provides an overview of the current understanding of the ubiquitin machinery from Legionella, highlighting structural and biochemical differences between the host-ubiquitin system and ubiquitin-related effectors.