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A nonphosphorylated 14-3-3 binding motif on exoenzyme S that is functional in vivo
Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine). (Bengt Hallberg)
Umeå University, Faculty of Science and Technology, Department of Molecular Biology (Faculty of Science and Technology). Umeå University, Faculty of Medicine, Umeå Centre for Microbial Research (UCMR). (Matthew Francis)
Umeå University, Faculty of Science and Technology, Department of Molecular Biology (Faculty of Science and Technology).
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2002 (English)In: European Journal of Biochemistry, ISSN 0014-2956, E-ISSN 1432-1033, Vol. 269, no 20, 4921-4929 p.Article in journal (Refereed) Published
Abstract [en]

14-3-3 proteins play an important role in a multitude of signalling pathways. The interactions between 14-3-3 and other signalling proteins, such as Raf and KSR (kinase suppressor of Ras), occur in a phospho-specific manner. Recently, a phosphorylation-independent interaction has been reported to occur between 14-3-3 and several proteins, for example 5-phosphatase, p75NTR-associated cell death executor (NADE) and the bacterial toxin Exoenzyme S (ExoS), an ADP-ribosyltransferase from Pseudomonas aeruginosa. In this study we have identified the amino acid residues on ExoS, which are responsible for its specific interaction with 14-3-3. Furthermore, we show that a peptide derived from ExoS, containing the 14-3-3 interaction site, effectively competes out the interaction between ExoS and 14-3-3. In addition, competition with this peptide blocks ExoS modification of Ras in our Ras modification assay. We show that the ExoS protein interacts with all isoforms of the 14-3-3 family tested. Moreover, in vivo an ExoS protein lacking the 14-3-3 binding site has a reduced capacity to ADP ribosylate cytoplasmic proteins, e.g. Ras, and shows a reduced capacity to change the morphology of infected cells.

Place, publisher, year, edition, pages
2002. Vol. 269, no 20, 4921-4929 p.
National Category
Medical and Health Sciences
Research subject
Biochemistry
Identifiers
URN: urn:nbn:se:umu:diva-59491DOI: DOI: 10.1046/j.1432-1033.2002.03191.xOAI: oai:DiVA.org:umu-59491DiVA: diva2:552685
Available from: 2012-09-14 Created: 2012-09-14 Last updated: 2017-12-07

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Publisher's full texthttp://onlinelibrary.wiley.com/doi/10.1046/j.1432-1033.2002.03191.x/full

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