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2. Multi-omic measurements of heterogeneity in HeLa cells across laboratories

Author

Liu, Yansheng, Mi, Yang, Mueller, Torsten, Kreibich, Saskia, Williams, Evan G., Van Drogen, Audrey, Borel, Christelle, Frank, Max, Germain, Pierre-Luc, Bludau, Isabell, Mehnert, Martin, Seifert, Michael, Emmenlauer, Mario, Sorg, Isabel, Bezrukov, Fedor, Bena, Frederique Sloan, Zhou, Hu, Dehio, Christoph, Testa, Giuseppe, Saez-Rodriguez, Julio, Antonarakis, Stylianos E., Hardt, Wolf-Dietrich, and Aebersold, Ruedi

Published
2019
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20. Genomic, Proteomic and Phenotypic Heterogeneity in HeLa Cells across Laboratories: Implications for Reproducibility of Research Results

Author

Liu, Yansheng, primary, Mi, Yang, additional, Mueller, Torsten, additional, Kreibich, Saskia, additional, Williams, Evan G., additional, Van Drogen, Audrey, additional, Borel, Christelle, additional, Germain, Pierre-Luc, additional, Frank, Max, additional, Bludau, Isabell, additional, Mehnert, Martin, additional, Seifert, Michael, additional, Emmenlauer, Mario, additional, Sorg, Isabel, additional, Bezrukov, Fedor, additional, Sloan Bena, Frederique, additional, Zhou, Hu, additional, Dehio, Christoph, additional, Testa, Giuseppe, additional, Saez-Rodriguez, Julio, additional, Antonarakis, Stylianos E., additional, Hardt, Wolf-Dietrich, additional, and Aebersold, Ruedi, additional

Published
2018
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21. Type III secretion: The bacteria-eukaryotic cell express

Author

Mota, Luís Jaime, Sorg, Isabel, Cornelis, Guy R., Mota, Luís Jaime, Sorg, Isabel, and Cornelis, Guy R.

Abstract

Type III secretion (T3S) is an export pathway used by Gram-negative pathogenic bacteria to inject bacterial proteins into the cytosol of eukaryotic host cells. This pathway is characterized by (i) a secretion nanomachine related to the bacterial flagellum, but usually topped by a stiff needle-like structure; (ii) the assembly in the eukaryotic cell membrane of a translocation pore formed by T3S substrates; (iii) a non-cleavable N-terminal secretion signal; (iv) T3S chaperones, assisting the secretion of some substrates; (v) a control mechanism ensuring protein delivery at the right place and time. Here, we review these different aspects focusing in open questions that promise exciting findings in the near future

Published
2017

22. Yersinia enterocolitica YopT and Clostridium difficile Toxin B Induce Expression of GILZ in Epithelial Cells

Author

Köberle, Martin, primary, Göppel, David, additional, Grandl, Tanja, additional, Gaentzsch, Peer, additional, Manncke, Birgit, additional, Berchtold, Susanne, additional, Müller, Steffen, additional, Lüscher, Bernhard, additional, Asselin-Labat, Marie-Liesse, additional, Pallardy, Marc, additional, Sorg, Isabel, additional, Langer, Simon, additional, Barth, Holger, additional, Zumbihl, Robert, additional, Autenrieth, Ingo B., additional, and Bohn, Erwin, additional

Published
2012
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29. Endocytosis-Independent Function of Clathrin Heavy Chain in the Control of Basal NF-κB Activation.

Author

Man Lyang Kim, Sorg, Isabel, and Arrieumerlou, Cécile

Subjects
*GENE expression, *CELL physiology, *ENDOCYTOSIS, *CELL growth, *CELL division, *IMMUNOFLUORESCENCE, *INTERLEUKIN-8, *EPITHELIAL cells
Abstract

Background: Nuclear factor-κB (NF-κB) is a transcription factor that regulates the transcription of genes involved in a variety of biological processes, including innate and adaptive immunity, stress responses and cell proliferation. Constitutive or excessive NF-κB activity has been associated with inflammatory disorders and higher risk of cancer. In contrast to the mechanisms controlling inducible activation, the regulation of basal NF-κB activation is not well understood. Here we test whether clathrin heavy chain (CHC) contributes to the regulation of basal NF-κB activity in epithelial cells. Methodology: Using RNA interference to reduce endogenous CHC expression, we found that CHC is required to prevent constitutive activation of NF-κB and gene expression. Immunofluorescence staining showed constitutive nuclear localization of the NF-κB subunit p65 in absence of stimulation after CHC knockdown. Elevated basal p65 nuclear localization is caused by constitutive phosphorylation and degradation of inhibitor of NF-κB alpha (IkBα) through an IκB kinase α (IKKα)-dependent mechanism. The role of CHC in NF-κB signaling is functionally relevant as constitutive expression of the proinflammatory chemokine interleukin-8 (IL-8), whose expression is regulated by NF-κB, was found after CHC knockdown. Disruption of clathrin-mediated endocytosis by chemical inhibition or depletion of the μ2-subunit of the endocytosis adaptor protein AP-2, and knockdown of clathrin light chain a (CHLa), failed to induce constitutive NF-κB activation and IL-8 expression, showing that CHC acts on NF-κB independently of endocytosis and CLCa. Conclusions: We conclude that CHC functions as a built-in molecular brake that ensures a tight control of basal NF-κB activation and gene expression in unstimulated cells. Furthermore, our data suggest a potential link between a defect in CHC expression and chronic inflammation disorder and cancer. [ABSTRACT FROM AUTHOR]

Published
2011
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30. Systems-Level Overview of Host Protein Phosphorylation During Shigella flexneriInfection Revealed by Phosphoproteomics*

Author

Schmutz, Christoph, Ahrné, Erik, Kasper, Christoph A., Tschon, Therese, Sorg, Isabel, Dreier, Roland F., Schmidt, Alexander, and Arrieumerlou, Cécile

Abstract

The enteroinvasive bacterium Shigella flexneriinvades the intestinal epithelium of humans. During infection, several injected effector proteins promote bacterial internalization, and interfere with multiple host cell responses. To obtain a systems-level overview of host signaling during infection, we analyzed the global dynamics of protein phosphorylation by liquid chromatography-tandem MS and identified several hundred of proteins undergoing a phosphorylation change during the first hours of infection. Functional bioinformatic analysis revealed that they were mostly related to the cytoskeleton, transcription, signal transduction, and cell cycle. Fuzzy c-means clustering identified six temporal profiles of phosphorylation and a functional module composed of ATM-phosphorylated proteins related to genotoxic stress. Pathway enrichment analysis defined mTOR as the most overrepresented pathway. We showed that mTOR complex 1 and 2 were required for S6 kinase and AKT activation, respectively. Comparison with a published phosphoproteome of Salmonella typhimurium-infected cells revealed a large subset of coregulated phosphoproteins. Finally, we showed that S. flexnerieffector OspF affected the phosphorylation of several hundred proteins, thereby demonstrating the wide-reaching impact of a single bacterial effector on the host signaling network.

Published
2013
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31. Recombinant YersiniaYopT Leads to Uncoupling of RhoA-Effector Interaction

Author

Sorg, Isabel, Goehring, Udo-Michael, Aktories, Klaus, and Schmidt, Gudula

Abstract

ABSTRACTYersinia enterocolitica, Yersinia pseudotuberculosis, and Yersinia pestisdeliver different Yop (Yersiniaouter proteins) effector proteins into mammalian cells by a type III secretion mechanism. Recently, it was shown thatYersiniaproducing YopT leads to disruption of the actin cytoskeleton of HeLa cells (M. Iriarte and G. R. Cornelis, Mol. Microbiol. 29:915–929, 1998). To analyze the molecular mechanism of YopT, we cloned and expressed YopT as a glutathioneS-transferase fusion protein. Recombinant YopT caused rounding up of embryonic bovine lung cells and redistribution of the actin cytoskeleton rapidly after microinjection. The Escherichia colicytotoxic necrotizing factor (CNF1), which constitutively activates Rho proteins, was not able to inhibit or revert YopT-induced cell rounding. YopT caused release of RhoA from embryonic bovine lung membranes and released recombinant isoprenylated RhoA from artificial PE or PE/PIP2 vesicles. Incubation of lysate or cytosol with YopT caused inhibition of the RhoA-rhotekin interaction but led to increased RhoA-RhoGDI interaction. It is suggested that inhibition of the interaction between RhoA and effectors is the underlying mechanism of the YopT action on the cytoskeleton.

Published
2001
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32. Yersinia enterocolitica YopT and Clostridium difficile toxin B induce expression of GILZ in epithelial cells

Author

Köberle, Martin, Göppel, David, Grandl, Tanja, Gaentzsch, Peer, Manncke, Birgit, Berchtold, Susanne, Müller, Steffen, Lüscher, Bernhard, Asselin-Labat, Marie-Liesse, Pallardy, Marc, Sorg, Isabel, Langer, Simon, Barth, Holger, Zumbihl, Robert, Autenrieth, Ingo B., and Bohn, Erwin

Subjects
3. Good health
Abstract

PLoS one 7(7), e40730 (2012). doi:10.1371/journal.pone.0040730, Published by PLoS [u.a.], Lawrence, Kan.

33. The helical content of the YscP molecular ruler determines the length of the Yersinia injectisome

Author

Wagner, Stefanie, Sorg, Isabel, Degiacomi, Matteo, Journet, Laure, Dal Peraro, Matteo, and Cornelis, Guy R.

Subjects
injectisome, YscP, molecular dynamics
Abstract

The length of the Yersinia injectisome needle is determined by the protein YscP, which could act as a molecular ruler. The analysis of the correlation between the size of YscP and the needle length in seven wild-type strains of Yersinia enterocolitica reinforced this hypothesis but hinted that the secondary structure of YscP might influence needle length. Hence, 11 variants of YscP515 were generated by multiple Pro or Gly substitutions. The needle length changed in inverse function of the helical content, indicating that not only the number of residues but also their structure controls length. Taking the secondary motifs into account, Pro/Gly-variants were subjected to in silico modelling to simulate the extension of YscP upon needle growth. The calculated lengths when the helical content is preserved correlated strikingly with the measured needle length, with a constant difference of ∼29 nm, which corresponds approximately to the size of the basal body. These data support the ruler model and show that the functional ruler has a helical structure.

34. Type III secretion: The bacteria-eukaryotic cell express

Author

Mota, Luís Jaime, Sorg, Isabel, Cornelis, Guy R., Mota, Luís Jaime, Sorg, Isabel, and Cornelis, Guy R.

Abstract

Type III secretion (T3S) is an export pathway used by Gram-negative pathogenic bacteria to inject bacterial proteins into the cytosol of eukaryotic host cells. This pathway is characterized by (i) a secretion nanomachine related to the bacterial flagellum, but usually topped by a stiff needle-like structure; (ii) the assembly in the eukaryotic cell membrane of a translocation pore formed by T3S substrates; (iii) a non-cleavable N-terminal secretion signal; (iv) T3S chaperones, assisting the secretion of some substrates; (v) a control mechanism ensuring protein delivery at the right place and time. Here, we review these different aspects focusing in open questions that promise exciting findings in the near future

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