@article{Schmitter2007Granu-7816,
  year={2007},
  doi={10.4049/​jimmunol.178.6.3797},
  title={The Granulocyte Receptor Carcinoembryonic Antigen-Related Cell Adhesion Molecule 3 (CEACAM3) Directly Associates with Vav to Promote Phagocytosis of Human Pathogens},
  number={6},
  volume={178},
  issn={0022-1767},
  journal={The Journal of Immunology},
  pages={3797--3805},
  author={Schmitter, Tim and Pils, Stefan and Sakk, Vadim and Frank, Ronald and Fischer, Klaus-Dieter and Hauck, Christof R.}
}

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    <dc:contributor>Sakk, Vadim</dc:contributor>
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    <dcterms:bibliographicCitation>First publ. in: The Journal of Immunology 178 (2007), 6, pp. 3797-3805</dcterms:bibliographicCitation>
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    <dc:creator>Frank, Ronald</dc:creator>
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    <dc:contributor>Pils, Stefan</dc:contributor>
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    <dcterms:title>The Granulocyte Receptor Carcinoembryonic Antigen-Related Cell Adhesion Molecule 3 (CEACAM3) Directly Associates with Vav to Promote Phagocytosis of Human Pathogens</dcterms:title>
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    <dc:creator>Hauck, Christof R.</dc:creator>
    <dc:creator>Schmitter, Tim</dc:creator>
    <dc:contributor>Hauck, Christof R.</dc:contributor>
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    <dc:creator>Pils, Stefan</dc:creator>
    <dc:contributor>Schmitter, Tim</dc:contributor>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:37:45Z</dc:date>
    <dcterms:abstract xml:lang="eng">The human granulocyte-specific receptor carcinoembryonic antigen-related cell adhesion molecule (CEACAM)3 is critically involved in the opsonin-independent recognition of several bacterial pathogens. CEACAM3-mediated phagocytosis depends on the integrity of an ITAM-like sequence within the cytoplasmic domain of CEACAM3 and is characterized by rapid stimulation of the GTPase Rac. By performing a functional screen with CEACAM3-expressing cells, we found that overexpression of a dominant-negative form of the guanine nucleotide exchange factor Vav, but not the dominant-negative versions SWAP70, Dock2, or ELMO1 interfered with CEACAM3-initiated phagocytosis. Moreover, small interfering RNA-mediated silencing of Vav reduced uptake and abrogated the stimulation of Rac in response to bacterial CEACAM3 engagement. In Vav1/Vav2-deficient cells, CEACAM3-mediated internalization was only observed after re-expression of Vav. Vav colocalized with CEACAM3 upon bacterial infection, coimmunoprecipitated in a complex with CEACAM3, and the Vav Src homology 2 domain directly associated with phosphorylated Tyr230 of CEACAM3. In primary human granulocytes, TAT-mediated transduction of dominant-negative Vav, but not SWAP70, severely impaired the uptake of CEACAM3-binding bacteria. These data support the view that, different from canonical ITAM signaling, the CEACAM3 ITAM-like sequence short-wires bacterial recognition and Rac stimulation via a direct association with Vav to promote rapid phagocytosis and elimination of CEACAM-binding human pathogens.</dcterms:abstract>
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    <dc:contributor>Frank, Ronald</dc:contributor>
    <dc:contributor>Fischer, Klaus-Dieter</dc:contributor>
    <dc:creator>Sakk, Vadim</dc:creator>
    <dc:creator>Fischer, Klaus-Dieter</dc:creator>
    <dcterms:issued>2007</dcterms:issued>
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