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Phagocytosis mediated by the human granulocyte receptor CEACAM3 is limited by the receptor-type protein tyrosine phosphatase PTPRJ

Phagocytosis mediated by the human granulocyte receptor CEACAM3 is limited by the receptor-type protein tyrosine phosphatase PTPRJ

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GOOB, Griseldis, Jonas ADRIAN, Chiara COSSU, Christof R. HAUCK, 2022. Phagocytosis mediated by the human granulocyte receptor CEACAM3 is limited by the receptor-type protein tyrosine phosphatase PTPRJ. In: Journal of Biological Chemistry. Elsevier. 298(9), 102269. ISSN 0021-9258. eISSN 1083-351X. Available under: doi: 10.1016/j.jbc.2022.102269

@article{Goob2022-09Phago-58069, title={Phagocytosis mediated by the human granulocyte receptor CEACAM3 is limited by the receptor-type protein tyrosine phosphatase PTPRJ}, year={2022}, doi={10.1016/j.jbc.2022.102269}, number={9}, volume={298}, issn={0021-9258}, journal={Journal of Biological Chemistry}, author={Goob, Griseldis and Adrian, Jonas and Cossu, Chiara and Hauck, Christof R.}, note={Article Number: 102269} }

<rdf:RDF xmlns:dcterms="http://purl.org/dc/terms/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#" xmlns:foaf="http://xmlns.com/foaf/0.1/" xmlns:void="http://rdfs.org/ns/void#" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/58069"> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dc:creator>Goob, Griseldis</dc:creator> <dcterms:rights rdf:resource="http://creativecommons.org/licenses/by-nc-nd/4.0/"/> <foaf:homepage rdf:resource="http://localhost:8080/jspui"/> <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/28"/> <dcterms:title>Phagocytosis mediated by the human granulocyte receptor CEACAM3 is limited by the receptor-type protein tyrosine phosphatase PTPRJ</dcterms:title> <dc:contributor>Adrian, Jonas</dc:contributor> <dc:creator>Hauck, Christof R.</dc:creator> <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/28"/> <dc:contributor>Cossu, Chiara</dc:contributor> <dc:contributor>Hauck, Christof R.</dc:contributor> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2022-07-19T07:40:35Z</dcterms:available> <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/58069/1/Goob_2-18lo7h9wwruw40.pdf"/> <dc:rights>Attribution-NonCommercial-NoDerivatives 4.0 International</dc:rights> <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/58069/1/Goob_2-18lo7h9wwruw40.pdf"/> <dcterms:abstract xml:lang="eng">Carcinoembryonic Antigen-related Cell Adhesion Molecule 3 (CEACAM3) is a human granulocyte receptor mediating the efficient phagocytosis of a subset of human-restricted bacterial pathogens. Its function depends on phosphorylation of a tyrosine-based sequence motif, but the enzyme(s) responsible for reversing this modification are unclear. Here, we identify the receptor-type protein tyrosine phosphatase PTPRJ as a negative regulator of CEACAM3-mediated phagocytosis. We show depletion of PTPRJ results in a gain-of-function phenotype, while overexpression of a constitutively active PTPRJ phosphatase strongly reduces bacterial uptake via CEACAM3. We also determined that recombinant PTPRJ directly dephosphorylates the cytoplasmic tyrosine residues of purified full-length CEACAM3 and recognizes synthetic CEACAM3-derived phospho-peptides as substrates. Dephosphorylation of CEACAM3 by PTPRJ is also observed in intact cells, thereby limiting receptor-initiated cytoskeletal re-arrangements, lamellipodia formation, and bacterial uptake. Finally, we show that human phagocytes deficient for PTPRJ exhibit exaggerated lamellipodia formation and enhanced opsonin-independent phagocytosis of CEACAM3-binding bacteria. Taken together, our results highlight PTPRJ as a bona fide negative regulator of CEACAM3-initiated phagocyte functions, revealing a potential molecular target to limit CEACAM3-driven inflammatory responses.</dcterms:abstract> <dc:contributor>Goob, Griseldis</dc:contributor> <dc:creator>Cossu, Chiara</dc:creator> <dc:creator>Adrian, Jonas</dc:creator> <dc:language>eng</dc:language> <dcterms:issued>2022-09</dcterms:issued> <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/58069"/> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2022-07-19T07:40:35Z</dc:date> </rdf:Description> </rdf:RDF>

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