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• W4285605718 endingPage "102269" @default.
• W4285605718 startingPage "102269" @default.
• W4285605718 abstract "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 phosphopeptides 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." @default.
• W4285605718 created "2022-07-16" @default.
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• W4285605718 date "2022-09-01" @default.
• W4285605718 modified "2023-09-30" @default.
• W4285605718 title "Phagocytosis mediated by the human granulocyte receptor CEACAM3 is limited by the receptor-type protein tyrosine phosphatase PTPRJ" @default.
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• W4285605718 doi "https://doi.org/10.1016/j.jbc.2022.102269" @default.
• W4285605718 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/35850306" @default.
• W4285605718 hasPublicationYear "2022" @default.
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