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@ARTICLE{Blasche:119665,
      author       = {S. Blasche$^*$ and S. Arens and A. Ceol and G. Siszler$^*$
                      and M. A. Schmidt and R. Häuser$^*$ and F. Schwarz$^*$ and
                      S. Wuchty and P. Aloy and P. Uetz and T. Stradal and M.
                      Koegl$^*$},
      title        = {{T}he {EHEC}-host interactome reveals novel targets for the
                      translocated intimin receptor.},
      journal      = {Scientific reports},
      volume       = {4},
      issn         = {2045-2322},
      address      = {London},
      publisher    = {Nature Publishing Group},
      reportid     = {DKFZ-2017-00296},
      pages        = {7531 -},
      year         = {2014},
      abstract     = {Enterohemorrhagic E. coli (EHEC) manipulate their human
                      host through at least 39 effector proteins which hijack host
                      processes through direct protein-protein interactions
                      (PPIs). To identify their protein targets in the host cells,
                      we performed yeast two-hybrid screens, allowing us to find
                      48 high-confidence protein-protein interactions between 15
                      EHEC effectors and 47 human host proteins. In comparison to
                      other bacteria and viruses we found that EHEC effectors bind
                      more frequently to hub proteins as well as to proteins that
                      participate in a higher number of protein complexes. The
                      data set includes six new interactions that involve the
                      translocated intimin receptor (TIR), namely HPCAL1, HPCAL4,
                      NCALD, ARRB1, PDE6D, and STK16. We compared these TIR
                      interactions in EHEC and enteropathogenic E. coli (EPEC) and
                      found that five interactions were conserved. Notably, the
                      conserved interactions included those of serine/threonine
                      kinase 16 (STK16), hippocalcin-like 1 (HPCAL1) as well as
                      neurocalcin-delta (NCALD). These proteins co-localize with
                      the infection sites of EPEC. Furthermore, our results
                      suggest putative functions of poorly characterized effectors
                      (EspJ, EspY1). In particular, we observed that EspJ is
                      connected to the microtubule system while EspY1 appears to
                      be involved in apoptosis/cell cycle regulation.},
      keywords     = {Adhesins, Bacterial (NLM Chemicals) / Escherichia coli
                      Proteins (NLM Chemicals) / EspJ protein, E coli (NLM
                      Chemicals) / HPCAL1 protein, human (NLM Chemicals) / NCALD
                      protein, human (NLM Chemicals) / Neurocalcin (NLM Chemicals)
                      / Receptors, Cell Surface (NLM Chemicals) / Tir protein, E
                      coli (NLM Chemicals) / Transcription Factors (NLM Chemicals)
                      / eaeA protein, E coli (NLM Chemicals) /
                      Protein-Serine-Threonine Kinases (NLM Chemicals) / STK16
                      protein, human (NLM Chemicals)},
      cin          = {W150},
      ddc          = {000},
      cid          = {I:(DE-He78)W150-20160331},
      pnm          = {312 - Functional and structural genomics (POF3-312)},
      pid          = {G:(DE-HGF)POF3-312},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:25519916},
      pmc          = {pmc:PMC4269881},
      doi          = {10.1038/srep07531},
      url          = {https://inrepo02.dkfz.de/record/119665},
}