Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 Glutamylation of Bacterial Ubiquitin Ligases by a Legionella Pseudokinase.

Literature DB >> 31624006

Glutamylation of Bacterial Ubiquitin Ligases by a Legionella Pseudokinase.

Alan G Sulpizio¹, Marena E Minelli¹, Yuxin Mao².

Abstract

Legionella pneumophila encodes a family of phosphoribosyl ubiquitination ligases (SidE) essential for the bacterium to establish successful infection. Four independent studies now show that the SidE family of ubiquitin ligases are regulated by a novel mechanism of glutamylation via a pseudokinase-like Legionella effector, SidJ, in an ATP- and calmodulin-dependent manner.

Entities: Chemical Disease Gene Species

Keywords: SdeA; SidE; SidJ; calmodulin; phosphoribosyl ubiquitination; post-translational modification

Mesh：

Substances：

Year: 2019 PMID： 31624006 PMCID： PMC7740076 DOI： 10.1016/j.tim.2019.09.001

Source DB: PubMed Journal: Trends Microbiol ISSN： 0966-842X Impact factor: 17.079

10 in total

1. Deubiquitination of phosphoribosyl-ubiquitin conjugates by phosphodiesterase-domain-containing Legionella effectors.

Authors: Min Wan; Alan G Sulpizio; Anil Akturk; Wendy H J Beck; Michael Lanz; Vitor M Faça; Marcus B Smolka; Joseph P Vogel; Yuxin Mao
Journal: Proc Natl Acad Sci U S A Date: 2019-11-05 Impact factor: 11.205

2. Bacterial pseudokinase catalyzes protein polyglutamylation to inhibit the SidE-family ubiquitin ligases.

Authors: Miles H Black; Adam Osinski; Marcin Gradowski; Kelly A Servage; Krzysztof Pawłowski; Diana R Tomchick; Vincent S Tagliabracci
Journal: Science Date: 2019-05-24 Impact factor: 47.728

3. Toxicity and SidJ-Mediated Suppression of Toxicity Require Distinct Regions in the SidE Family of Legionella pneumophila Effectors.

Authors: James C Havey; Craig R Roy
Journal: Infect Immun Date: 2015-06-22 Impact factor: 3.441

4. Phosphoribosylation of Ubiquitin Promotes Serine Ubiquitination and Impairs Conventional Ubiquitination.

Authors: Sagar Bhogaraju; Sissy Kalayil; Yaobin Liu; Florian Bonn; Thomas Colby; Ivan Matic; Ivan Dikic
Journal: Cell Date: 2016-12-01 Impact factor: 41.582

5. A Single Legionella Effector Catalyzes a Multistep Ubiquitination Pathway to Rearrange Tubular Endoplasmic Reticulum for Replication.

Authors: Kristin M Kotewicz; Vinay Ramabhadran; Nicole Sjoblom; Joseph P Vogel; Eva Haenssler; Mengyun Zhang; Jessica Behringer; Rebecca A Scheck; Ralph R Isberg
Journal: Cell Host Microbe Date: 2016-12-29 Impact factor: 21.023

6. Spatiotemporal regulation of a Legionella pneumophila T4SS substrate by the metaeffector SidJ.

Authors: Kwang Cheol Jeong; Jessica A Sexton; Joseph P Vogel
Journal: PLoS Pathog Date: 2015-03-16 Impact factor: 6.823

7. Regulation of phosphoribosyl ubiquitination by a calmodulin-dependent glutamylase.

Authors: Ninghai Gan; Xiangkai Zhen; Yao Liu; Xiaolong Xu; Chunlin He; Jiazhang Qiu; Yancheng Liu; Grant M Fujimoto; Ernesto S Nakayasu; Biao Zhou; Lan Zhao; Kedar Puvar; Chittaranjan Das; Songying Ouyang; Zhao-Qing Luo
Journal: Nature Date: 2019-07-22 Impact factor: 49.962

8. Protein polyglutamylation catalyzed by the bacterial calmodulin-dependent pseudokinase SidJ.

Authors: Alan Sulpizio; Marena E Minelli; Min Wan; Paul D Burrowes; Xiaochun Wu; Ethan J Sanford; Jung-Ho Shin; Byron C Williams; Michael L Goldberg; Marcus B Smolka; Yuxin Mao
Journal: Elife Date: 2019-11-04 Impact factor: 8.140

9. Ubiquitination independent of E1 and E2 enzymes by bacterial effectors.

Authors: Jiazhang Qiu; Michael J Sheedlo; Kaiwen Yu; Yunhao Tan; Ernesto S Nakayasu; Chittaranjan Das; Xiaoyun Liu; Zhao-Qing Luo
Journal: Nature Date: 2016-04-06 Impact factor: 49.962

10. Inhibition of bacterial ubiquitin ligases by SidJ-calmodulin catalysed glutamylation.

Authors: Sagar Bhogaraju; Florian Bonn; Rukmini Mukherjee; Michael Adams; Moritz M Pfleiderer; Wojciech P Galej; Vigor Matkovic; Jaime Lopez-Mosqueda; Sissy Kalayil; Donghyuk Shin; Ivan Dikic
Journal: Nature Date: 2019-07-22 Impact factor: 49.962

10 in total

5 in total

Glutamylation of Bacterial Ubiquitin Ligases by a Legionella Pseudokinase.

1. Deubiquitination of phosphoribosyl-ubiquitin conjugates by phosphodiesterase-domain-containing Legionella effectors.

2. Bacterial pseudokinase catalyzes protein polyglutamylation to inhibit the SidE-family ubiquitin ligases.

3. Toxicity and SidJ-Mediated Suppression of Toxicity Require Distinct Regions in the SidE Family of Legionella pneumophila Effectors.

4. Phosphoribosylation of Ubiquitin Promotes Serine Ubiquitination and Impairs Conventional Ubiquitination.

5. A Single Legionella Effector Catalyzes a Multistep Ubiquitination Pathway to Rearrange Tubular Endoplasmic Reticulum for Replication.

6. Spatiotemporal regulation of a Legionella pneumophila T4SS substrate by the metaeffector SidJ.

7. Regulation of phosphoribosyl ubiquitination by a calmodulin-dependent glutamylase.

8. Protein polyglutamylation catalyzed by the bacterial calmodulin-dependent pseudokinase SidJ.

9. Ubiquitination independent of E1 and E2 enzymes by bacterial effectors.

10. Inhibition of bacterial ubiquitin ligases by SidJ-calmodulin catalysed glutamylation.

1. Legionella pneumophila balances ubiquitin transglutamination.

Review 2. Looking lively: emerging principles of pseudokinase signaling.

Review 3. Polyglutamylation: biology and analysis.

Review 4. Pathogenicity and Virulence of Legionella: Intracellular replication and host response.

Review 5. Glycosylating Effectors of Legionella pneumophila: Finding the Sweet Spots for Host Cell Subversion.