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Receptor Clustering in Monocytes1
Departments of
*
Internal Medicine and
Microbiology, Ohio State University, Columbus, OH 43210
Current models of Fc
R signal transduction in monocytes describe
a molecular cascade that begins upon clustering of FcR with the
phosphorylation of critical tyrosine residues in the cytoplasmic
domains of FcRIIa or the -chain subunit of FcRI and
FcRIIIa. The cascade engages several other tyrosine-phosphorylated
molecules, either enzymes or adapters, to manifest ultimately an array
of biological responses, including phagocytosis, cell killing,
secretion of a variety of inflammatory mediators, and activation.
Continuing to assess systematically the molecules participating in the
cascade, we have found that the SH2-containing 5'-inositol phosphatase
(SHIP) is phosphorylated on tyrosine early and transiently after FcR
clustering. This molecule in other systems, such as B cells and mast
cells, mediates an inhibitory signal. We find that clustering of either
FcRIIa or FcRI is effective in inducing SHIP phosphorylation,
that SHIP binds in vitro to a phosphorylated immunoreceptor
tyrosine-based activation motif, peptide from the cytoplasmic domain of
FcRIIa in activation-independent fashion, although SHIP binding
increases upon cell activation, and that FcRIIb and FcRIIc are
not responsible for the observed SHIP phosphorylation. These findings
prompt us to propose that SHIP inhibits FcR-mediated signal
transduction by engaging immunoreceptor tyrosine-based activation
motif-containing cytoplasmic domains of FcRIIa and
FcRI-associated -chain.
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