Abstract
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 autophagymediated 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 proteins 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 Legionella.
Original language | English |
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Pages (from-to) | 316-322 |
Number of pages | 7 |
Journal | BMB reports |
Volume | 55 |
Issue number | 7 |
DOIs | |
Publication status | Published - 2022 |
Bibliographical note
Funding Information:This work was supported by a National Research Foundation of Korea (NRF) grant funded by the Korean government (MSIT) (No. 2021R1C1C100396112 and 2018R1A6A1A0302560722) and the Yonsei University Research Fund of 2021 (2021-22-0050).
Publisher Copyright:
© 2022. by the The Korean Society for Biochemistry and Molecular Biology
All Science Journal Classification (ASJC) codes
- Biochemistry
- Molecular Biology