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Tyrosine phosphorylation and Fcγ receptor‐mediated phagocytosis
Author(s) -
Strzelecka Agnieszka,
Kwiatkowska Katarzyna,
Sobota Andrzej
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01359-2
Subject(s) - immunoreceptor tyrosine based activation motif , syk , tyrosine phosphorylation , internalization , phosphorylation , microbiology and biotechnology , tyrosine , proto oncogene tyrosine protein kinase src , sh2 domain , opsonin , receptor , receptor tyrosine kinase , signal transduction , phagocytosis , tyrosine kinase , chemistry , protein tyrosine phosphatase , biochemistry , biology
Phagocytosis of IgG‐opsonized particulate material in hematopoietic cells is mediated by Fcγ receptors (FcγRs). Interaction of the receptors with Fc domains of IgG triggers transduction of phagocytic signal in which a key role is played by phosphorylation of tyrosine residues of the receptors. These residues are arranged into a specific motif (immunoreceptor tyrosine‐based activation motif; ITAM) which is located either in the cytoplasmic part of FcγRIIA or in γ chains associated with FcγRI and FcγRIIIA. The conserved tyrosine residues are phosphorylated by, and associate with, tyrosine kinases of Src and Syk families. Coordinated action of these components initiates numerous intracellular events leading finally to local rearrangement of the actin‐based cytoskeleton and internalization of the particles.