Ubiquitin-regulating effector proteins from Legionella
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초록
Ubiquitin is relatively modest in size but involves almost entirecellular signaling pathways. The primary role of ubiquitin ismaintaining cellular protein homeostasis. Ubiquitination regulatesthe fate of target proteins using the proteasome- or autophagymediateddegradation of ubiquitinated substrates, which can beeither intracellular or foreign proteins from invading pathogens. Legionella, a gram-negative intracellular pathogen, hinders thehost-ubiquitin system by translocating hundreds of effector proteinsinto the host cell’s cytoplasm. In this review, we describethe current understanding of ubiquitin machinery from Legionella. We summarize structural and biochemical differences betweenthe host-ubiquitin system and ubiquitin-related effectors of Legionella. Some of these effectors act much like canonical host-ubiquitinmachinery, whereas others have distinctive structures andaccomplish non-canonical ubiquitination via novel biochemicalmechanisms.
Abstract
Ubiquitin is relatively modest in size but involves almost entirecellular signaling pathways. The primary role of ubiquitin ismaintaining cellular protein homeostasis. Ubiquitination regulatesthe fate of target proteins using the proteasome- or autophagymediateddegradation of ubiquitinated substrates, which can beeither intracellular or foreign proteins from invading pathogens. Legionella, a gram-negative intracellular pathogen, hinders thehost-ubiquitin system by translocating hundreds of effector proteinsinto the host cell’s cytoplasm. In this review, we describethe current understanding of ubiquitin machinery from Legionella. We summarize structural and biochemical differences betweenthe host-ubiquitin system and ubiquitin-related effectors of Legionella. Some of these effectors act much like canonical host-ubiquitinmachinery, whereas others have distinctive structures andaccomplish non-canonical ubiquitination via novel biochemicalmechanisms.
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