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Subunit Immunoreceptor Tyrosine-Based Activation Motif in Signaling of Myeloid High Affinity Fc Receptor for IgG (FcRI)1
*
Neil Bogart Memorial Laboratories, Division of Hematology-Oncology, and
Section of Molecular Carcinogenesis, Department of Pathology, Childrens Hospital Los Angeles Research Institute and University of Southern California School of Medicine, Los Angeles, CA 90027; and
Department of Microbiology and Immunology, Wonkwang University School of Medicine, Iksan Jeonbuk, Korea
Cbl-Crkl and Crkl-C3G interactions have been implicated in T cell
and B cell receptor signaling and in the regulation of the small
GTPase, Rap1. Recent evidence suggests that Rap1 plays a prominent role
in the regulation of immunoreceptor tyrosine-based activation motif
(ITAM) signaling. To gain insight into the role of Crkl in myeloid ITAM
signaling, we investigated Cbl-Crkl and Crkl-C3G interactions following
Fc
RI aggregation in U937IF cells. FcRI cross-linking of U937IF
cells results in the tyrosine phosphorylation of Cbl, Crkl, and Hef-1,
an increase in the association of Crkl with Cbl via direct SH2 domain
interaction and increased Crkl-Hef-1 binding. Crkl constitutively binds
to the guanine nucleotide-releasing protein, C3G, via direct SH3 domain
binding. Our data show that distinct Cbl-Crkl and Crkl-C3G complexes
exist in myeloid cells, suggesting that these complexes may modulate
distinct signaling events. Anti-Crkl immunoprecipitations demonstrate
that the ITAM-containing subunit of FcRI is induced to form a
complex with the Crkl protein, and Crkl binds to the cytoskeletal
protein, Hef-1. The induced association of Crkl with Cbl, Hef-1, and
FcRI after FcRI activation and the constitutive association
between C3G and Crkl provide the first evidence that a
FcRI-Crkl-C3G complex may link ITAM receptors to the activation
of Rap1 in myeloid cells.
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