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The Journal of Immunology, Vol 152, Issue 11 5429-5437, Copyright © 1994 by American Association of Immunologists
ARTICLES |
C Darby, RL Geahlen and AD Schreiber
Graduate Group in Immunology, University of Pennsylvania, Philadelphia 19104.
The role of tyrosine phosphorylation during signal transduction by the phagocytic macrophage (Mphi) FcR Fc gamma RIIIA was investigated. Cross- linking Fc gamma RIIIA on pulmonary Mphi or cultured monocytes used as in vitro model for differentiated Mphi induced rapid and transient phosphorylation of multiple protein substrates. The lymphocyte/mast cell 72-kDa protein tyrosine kinase (PTK) designated PTK72 or Syk, whose expression in Mphi was previously unknown, was identified as a major substrate by immunoprecipitation and phosphopeptide mapping. Activation of Fc gamma RIIIA stimulated a fourfold increase in Syk kinase activity assessed by autophosphorylation. Under mild lysis conditions several specific proteins were co-precipitated with the gamma subunit of Fc gamma RIIIA. Tyrosine kinase activity was also co- precipitated with gamma, as shown by in vitro phosphorylation of gamma. One of these kinases was identified as Syk by phosphopeptide mapping, suggesting a physical association between this PTK and the receptor. Two additional phosphoproteins induced by Fc gamma RIIIA cross-linking were identified: the hematopoietic proto-oncogene product p95Vav, previously implicated in B lymphocyte and mast cell signaling; and p62, a protein associated with p21Ras-GAP. Our results also establish that there are important functional similarities in signal transduction between a phagocytic Mphi FcR and other multi-subunit Ig gene family receptors in diverse cell lineages.
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J. D. Peters, M. T. Furlong, D. J. Asai, M. L. Harrison, and R. L. Geahlen Syk, Activated by Cross-linking the B-cell Antigen Receptor, Localizes to the Cytosol Where It Interacts with and Phosphorylates alpha-Tubulin on Tyrosine J. Biol. Chem., March 1, 1996; 271(9): 4755 - 4762. [Abstract] [Full Text] [PDF]
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J. Fargnoli, A. L. Burkhardt, M. Laverty, S. A. Kut, N. S. C. van Oers, A. Weiss, and J. B. Bolen Syk Mutation in Jurkat E6-derived Clones Results in Lack of p72[IMAGE] Expression J. Biol. Chem., November 3, 1995; 270(44): 26533 - 26537. [Abstract] [Full Text] [PDF]
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T. H. Lin, C. Rosales, K. Mondal, J. B. Bolen, S. Haskill, and R. L. Juliano Integrin-mediated Tyrosine Phosphorylation and Cytokine Message Induction in Monocytic Cells J. Biol. Chem., July 7, 1995; 270(27): 16189 - 16197. [Abstract] [Full Text] [PDF]
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L. L. Wang, S.ép. Richard, and A. S. Shaw p62 Association with RNA Is Regulated by Tyrosine Phosphorylation J. Biol. Chem., February 3, 1995; 270(5): 2010 - 2013. [Abstract] [Full Text] [PDF]
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Z. Songyang, Y. Yamanashi, D. Liu, and D. Baltimore Domain-dependent Function of the rasGAP-binding Protein p62Dok in Cell Signaling J. Biol. Chem., January 19, 2001; 276(4): 2459 - 2465. [Abstract] [Full Text] [PDF]
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