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Cited by 238Phagocytosis and Immune RegulationMonoclonal and Polyclonal Antibodies ResearchCell Adhesion Molecules Research

The DOI matches its Crossref record; 51 of the 51 references it cites were found in a registry or an index.

Tyrosine phosphorylation of the gamma subunit of Fc gamma receptors, p72syk, and paxillin during Fc receptor-mediated phagocytosis in macrophages.

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Greenberg, S., Chang, P., Silverstein, S.C.·1994·Journal of Biological Chemistry
DOI 10.1016/s0021-9258(17)41945-4
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Abstract

Fc receptor-mediated phagocytosis in mouse macrophages occurs by a tyrosine kinase-dependent pathway (Greenberg, S., Chang, P., and Silverstein, S.C. (1993) J. Exp. Med. 177, 529-534). To identify proteins that are phosphorylated on tyrosine residues during phagocytosis, we used anti-phosphotyrosine antibodies to perform immunoblotting and immunoprecipitation of lysates derived from Fc receptor-stimulated macrophages. Proteins of 26, 30, 35, 37, 40, 43, 47, 56, 60, 68, 83, 116, and 150 kDa displayed enhanced tyrosine phosphorylation during Fc receptor-mediated phagocytosis. Tyrosine phosphorylation of these proteins was not a consequence of actin polymerization since treatment with cytochalasin D did not alter the pattern of Fc receptor-stimulated protein tyrosine phosphorylation. The 68-kDa tyrosine phosphoprotein was identified as paxillin, a cytoskeletal-associated tyrosine kinase substrate previously identified in fibroblasts and shown to localize to focal adhesions (Turner, C.E., Glenney, J.R., and Burridge, K. (1990) J. Cell Biol. 111, 1059-1068). Paxillin colocalized with F-actin beneath nascent phagosomes. In addition to the above proteins detected by anti-phosphotyrosine immunoblotting, the gamma subunit of FcRI and III was shown to undergo tyrosine phosphorylation during Fc receptor-mediated phagocytosis. Of several candidate tyrosine kinases that may be activated during Fc receptor stimulation, p72syk, but not p125FAK, displayed enhanced tyrosine phosphorylation du…

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Crossref · 10.1016/s0021-9258(17)41945-4

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  1. Huang, 1990, Biochem. J., 269, 136

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Metadata

Authors
Greenberg, S., Chang, P., & Silverstein, S. C.
Affiliations
Columbia University (US)
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1994-02
Volume
269
Issue
5
Pages
3897-3902
ISSN
0021-9258 (ISSN-L)
DOI
10.1016/s0021-9258(17)41945-4
OpenAlex
W1545383294
Cited by
237
References
51
Citations by year
2023: 1 · 2022: 1 · 2021: 7 · 2020: 1 · 2019: 2 · 2018: 1 · 2017: 1 · 2016: 3 · 2015: 4 · 2014: 9 · 2012: 3
FWCI
10.15
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health (5k08hl002641-04)
  • National Heart, Lung, and Blood Institute (HL 02641)
  • National Institute of Allergy and Infectious Diseases (AI20516)
Topics
  • Life Sciences › Immunology and Microbiology › Immunology › Phagocytosis and Immune Regulation
  • Life Sciences › Immunology and Microbiology › Immunology › Monoclonal and Polyclonal Antibodies Research
  • Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
Keywords
tyrosine phosphorylation, Fc gamma receptor, p72syk, paxillin, phagocytosis, macrophages, cytoskeleton, focal adhesions, F-actin, tyrosine kinase substrate, p125FAK
MeSH terms
Actins, Animals, Chromatography, Affinity, Cytoskeletal Proteins, Electrophoresis, Polyacrylamide Gel, Fluorescent Antibody Technique, Mice, Inbred C57BL, Models, Biological, Molecular Weight, Phagocytosis, Phosphoproteins, Phosphorylation, Protein-Tyrosine Kinases, Tyrosine, Cytochalasin D, Receptors, IgG, Macrophages, Peritoneal, Phosphotyrosine, Macromolecular Substances, Mice, Paxillin

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