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Literature DB >> 31994202

Legionella pneumophila balances ubiquitin transglutamination.

Fujie Yan^1,2, Yongqun Zhu^1,2,3, Yan Zhou¹.

Abstract

The effector MavC of the bacterial pathogen Legionella pneumophila catalyzes a noncanonical ubiquitination of the host ubiquitin-conjugating E2 enzyme UBE2N by crosslinking a glutamine residue of ubiquitin to UBE2N lysine residues via its transglutaminase activity. A new study by Gan et al (2020) reveals that L. pneumophila reverses this noncanonical ubiquitination via its ubiquitin deamidase effector MvcA to allow precise temporal regulation of host signaling during infection.

Entities: Chemical Disease Species

Mesh：

Substances：

Year: 2020 PMID： 31994202 PMCID： PMC7024833 DOI： 10.15252/embj.2019104258

Source DB: PubMed Journal: EMBO J ISSN： 0261-4189 Impact factor: 11.598

11 in total

Review 1. Modification of proteins by ubiquitin and ubiquitin-like proteins.

Authors: Oliver Kerscher; Rachael Felberbaum; Mark Hochstrasser
Journal: Annu Rev Cell Dev Biol Date: 2006 Impact factor: 13.827

2. A bacterial effector deubiquitinase specifically hydrolyses linear ubiquitin chains to inhibit host inflammatory signalling.

Authors: Muyang Wan; Xiaofei Wang; Chunfeng Huang; Dandan Xu; Zhao Wang; Yan Zhou; Yongqun Zhu
Journal: Nat Microbiol Date: 2019-05-20 Impact factor: 17.745

3. Legionella pneumophila regulates the activity of UBE2N by deamidase-mediated deubiquitination.

Authors: Ninghai Gan; Hongxin Guan; Yini Huang; Ting Yu; Jiaqi Fu; Ernesto S Nakayasu; Kedar Puvar; Chittaranjan Das; Dongmei Wang; Songying Ouyang; Zhao-Qing Luo
Journal: EMBO J Date: 2019-12-11 Impact factor: 11.598

4. Legionella pneumophila balances ubiquitin transglutamination.

Authors: Fujie Yan; Yongqun Zhu; Yan Zhou
Journal: EMBO J Date: 2020-01-28 Impact factor: 11.598

5. Host proteasomal degradation generates amino acids essential for intracellular bacterial growth.

Authors: Christopher T D Price; Tasneem Al-Quadan; Marina Santic; Ilan Rosenshine; Yousef Abu Kwaik
Journal: Science Date: 2011-11-17 Impact factor: 47.728

Review 6. Modulation of small GTPases by Legionella.

Authors: Roger S Goody; Aymelt Itzen
Journal: Curr Top Microbiol Immunol Date: 2013 Impact factor: 4.291

7. Discovery of Ubiquitin Deamidases in the Pathogenic Arsenal of Legionella pneumophila.

Authors: Dylan Valleau; Andrew T Quaile; Hong Cui; Xiaohui Xu; Elena Evdokimova; Changsoo Chang; Marianne E Cuff; Malene L Urbanus; Scott Houliston; Cheryl H Arrowsmith; Alexander W Ensminger; Alexei Savchenko
Journal: Cell Rep Date: 2018-04-10 Impact factor: 9.423

Legionella pneumophila balances ubiquitin transglutamination.

Review 1. Modification of proteins by ubiquitin and ubiquitin-like proteins.

2. A bacterial effector deubiquitinase specifically hydrolyses linear ubiquitin chains to inhibit host inflammatory signalling.

3. Legionella pneumophila regulates the activity of UBE2N by deamidase-mediated deubiquitination.

4. Legionella pneumophila balances ubiquitin transglutamination.

5. Host proteasomal degradation generates amino acids essential for intracellular bacterial growth.

Review 6. Modulation of small GTPases by Legionella.

7. Discovery of Ubiquitin Deamidases in the Pathogenic Arsenal of Legionella pneumophila.

8. Glutamylation of Bacterial Ubiquitin Ligases by a Legionella Pseudokinase.

9. Legionella pneumophila inhibits immune signalling via MavC-mediated transglutaminase-induced ubiquitination of UBE2N.

Review 10. The Legionella pneumophila replication vacuole: making a cosy niche inside host cells.

1. Legionella pneumophila balances ubiquitin transglutamination.