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Protein tyrosine phosphorylation in leukocyte activation through receptors for IgG
Author(s) -
Santana Carla,
Noris Gino,
Espinoza Bertha,
Ortega Enrique
Publication year - 1996
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1002/jlb.60.4.433
Subject(s) - biology , tyrosine phosphorylation , phosphorylation , receptor , immunology , microbiology and biotechnology , protein tyrosine phosphatase , tyrosine , protein phosphorylation , biochemistry , protein kinase a
Membrane receptors for the Fc portion of immunoglobulin G (IgG) antibodies (FcγRs) are expressed on almost every type of hematopoietic cells, where they mediate a wide variety of effector functions. A high degree of structural heterogeneity exists among FcγRs. The biological significance of such heterogeneity is unknown, since the structural diversity does not appear to be reflected in the binding specificity nor in the effector functions that each distinct receptor is able to mediate. Recent work has emphasized the essential role of protein tyrosine phosphorylation in the initiation of trans‐membrane signaling by these receptors. In this article we review the role of protein tyrosine phosphorylation in signal transduction by the different types of FcγRs in order to assess to what extent the structural heterogeneity of this receptor family is related to different activation pathways utilized by each of its members. J. Leukoc. Biol . 60: 433–440; 1996.