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Cutting Edge |
RI
*
Division of Hygienic Chemistry, Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan; and
Department of Oncogene Research, Research Institute for Microbial Diseases, Osaka University, Osaka, Japan
Tyrosine phosphorylation in the cytoplasmic
domains of Fc
RI by the Src family kinase Lyn initiates a signaling
cascade leading to mast cell activation. In this study, we show that a
recently identified transmembrane protein, Csk-binding protein (Cbp),
also known as phospoprotein associated with glycosphingolipid-enriched
microdomains (PAG), negatively regulates FcRI signaling. In rat
basophilic leukemia (RBL)-2H3 cells, the levels of tyrosine
phosphorylation of Cbp/PAG and its association with
Csk, a negative regulator for Lyn, significantly elevate immediately
after aggregation of FcRI. An overexpression of Cbp/PAG in RBL-2H3
cells inhibits FcRI-mediated cell activation. This is accompanied
with decreased levels of tyrosine phosphorylation of
FcRI, association of FcRI with Lyn, and FcRI-associated
tyrosine kinase activity. These findings combined with the fact that
Cbp/PAG, Lyn, and aggregated FcRI are localized to lipid rafts,
suggest that upon FcRI aggregation Cbp/PAG down-regulates the
receptor-associated Lyn activity through relocating Csk to rafts,
thereby efficiently mediating feedback inhibition of FcRI
signaling.
This article has been cited by other articles:
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