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The Escherichia coli effector EspJ blocks Src kinase activity via amidation and ADP ribosylation

Please always quote using this URN: urn:nbn:de:bvb:20-opus-121157
  • The hallmark of enteropathogenic Escherichia coli (EPEC) infection is the formation of actin-rich pedestal-like structures, which are generated following phosphorylation of the bacterial effector Tir by cellular Src and Abl family tyrosine kinases. This leads to recruitment of the Nck-WIP-N-WASP complex that triggers Arp2/3-dependent actin polymerization in the host cell. The same phosphorylation-mediated signalling network is also assembled downstream of the Vaccinia virus protein A36 and the phagocytic Fc-gamma receptor FcγRIIa. Here weThe hallmark of enteropathogenic Escherichia coli (EPEC) infection is the formation of actin-rich pedestal-like structures, which are generated following phosphorylation of the bacterial effector Tir by cellular Src and Abl family tyrosine kinases. This leads to recruitment of the Nck-WIP-N-WASP complex that triggers Arp2/3-dependent actin polymerization in the host cell. The same phosphorylation-mediated signalling network is also assembled downstream of the Vaccinia virus protein A36 and the phagocytic Fc-gamma receptor FcγRIIa. Here we report that the EPEC type-III secretion system effector EspJ inhibits autophosphorylation of Src and phosphorylation of the Src substrates Tir and FcγRIIa. Consistent with this, EspJ inhibits actin polymerization downstream of EPEC, Vaccinia virus and opsonized red blood cells. We identify EspJ as a unique adenosine diphosphate (ADP) ribosyltransferase that directly inhibits Src kinase by simultaneous amidation and ADP ribosylation of the conserved kinase-domain residue, Src E310, resulting in glutamine-ADP ribose.show moreshow less

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Metadaten
Author: Joanna C. Young, Abigail Clements, Alexander E. Lang, James A. Garnett, Diana Munera, Ana Arbeloa, Jaclyn Pearson, Elizabeth L. Hartland, Stephen J. Matthews, Aurelie Mousnier, David J. Barry, Michael Way, Andreas Schlosser, Klaus Aktories, Gad Frankel
URN:urn:nbn:de:bvb:20-opus-121157
Document Type:Journal article
Faculties:Fakultät für Biologie / Rudolf-Virchow-Zentrum
Language:English
Parent Title (English):Nature Communications
Year of Completion:2014
Volume:5
Issue:5887
Source:Nature Communications 5:5887 doi: 10.1038/ncomms6887 (2014).
DOI:https://doi.org/10.1038/ncomms6887
Pubmed Id:http://www.ncbi.nlm.nih.gov/pubmed?term=25523213
Dewey Decimal Classification:6 Technik, Medizin, angewandte Wissenschaften / 61 Medizin und Gesundheit / 610 Medizin und Gesundheit
Release Date:2016/02/17
Licence (German):License LogoCC BY: Creative-Commons-Lizenz: Namensnennung