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  Regulation of Phosphoribosyl-Linked Serine Ubiquitination by Deubiquitinases DupA and DupB

Shin, D., Mukherjee, R., Liu, Y., Gonzalez, A., Bonn, F., Liu, Y., et al. (2020). Regulation of Phosphoribosyl-Linked Serine Ubiquitination by Deubiquitinases DupA and DupB. Molecular Cell, 77(1), 164-179. doi:10.1016/j.molcel.2019.10.019.

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https://doi.org/10.1016/j.molcel.2019.10.019 (Publisher version)
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 Creators:
Shin, Donghyuk1, 2, 3, Author              
Mukherjee, Rukmini2, 3, Author
Liu, Yaobin2, 3, Author
Gonzalez, Alexis2, 3, Author
Bonn, Florian2, Author
Liu, Yan4, Author
Rogov, Vladimir V.5, Author
Heinz, Marcel6, 7, Author              
Stolz, Alexandra2, 3, Author
Hummer, Gerhard6, 7, Author              
Dötsch, Volker5, Author
Luo, Zhao-Qing4, Author
Bhogaraju, Sagar2, 3, 8, Author
Đikić, Ivan1, 2, 3, Author              
Affiliations:
1Max Planck Fellow Group ER remodelling Group, Prof. Ivan Đikić, Max Planck Institute of Biophysics, Max Planck Society, ou_3004983              
2Institute of Biochemistry II, Faculty of Medicine, Goethe University Frankfurt, Frankfurt am Main, Germany, ou_persistent22              
3Buchmann Institute for Molecular Life Sciences, Goethe University Frankfurt, Frankfurt am Main, Germany, ou_persistent22              
4Purdue Institute of Immunology, Inflammation, and Infectious Diseases and Department of Biological Sciences, Purdue University, West Lafayette, USA, ou_persistent22              
5Institute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance and Cluster of Excellence Macromolecular Complexes (CEF), Goethe University, Frankfurt, Germany, ou_persistent22              
6Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society, ou_2068292              
7Institute of Biophysics, Goethe University Frankfurt, Frankfurt am Main, Germany, ou_persistent22              
8European Molecular Biology Laboratory, Grenoble, France, ou_persistent22              

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Free keywords: ADP-ribosylation, deubiquitinase, deubiquitination, endoplasmic reticulum, ER-fragmentation, Legionella pneumophila, phosphodiesterase, phosphoribosyl serine ubiquitination, SdeA
 Abstract: The family of bacterial SidE enzymes catalyzes non-canonical phosphoribosyl-linked (PR) serine ubiquitination and promotes infectivity of Legionella pneumophila. Here, we describe identification of two bacterial effectors that reverse PR ubiquitination and are thus named deubiquitinases for PR ubiquitination (DUPs; DupA and DupB). Structural analyses revealed that DupA and SidE ubiquitin ligases harbor a highly homologous catalytic phosphodiesterase (PDE) domain. However, unlike SidE ubiquitin ligases, DupA displays increased affinity to PR-ubiquitinated substrates, which allows DupA to cleave PR ubiquitin from substrates. Interfering with DupA-ubiquitin binding switches its activity toward SidE-type ligase. Given the high affinity of DupA to PR-ubiquitinated substrates, we exploited a catalytically inactive DupA mutant to trap and identify more than 180 PR-ubiquitinated host proteins in Legionella-infected cells. Proteins involved in endoplasmic reticulum (ER) fragmentation and membrane recruitment to Legionella-containing vacuoles (LCV) emerged as major SidE targets. The global map of PR-ubiquitinated substrates provides critical insights into host-pathogen interactions during Legionella infection.

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Language(s): eng - English
 Dates: 2019-09-072019-06-062019-10-112019-11-122020-01-02
 Publication Status: Published in print
 Pages: 16
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.molcel.2019.10.019
BibTex Citekey: shin_regulation_2019
 Degree: -

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Title: Molecular Cell
Source Genre: Journal
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Publ. Info: Cambridge, Mass. : Cell Press
Pages: - Volume / Issue: 77 (1) Sequence Number: - Start / End Page: 164 - 179 Identifier: ISSN: 1097-2765
CoNE: https://pure.mpg.de/cone/journals/resource/954925610929