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-Kinase to the Integrin Signaling Pathway
(Received for publication, July 22, 1996, and in revised form, October 11, 1996)
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From the Integrin-mediated cell adhesion triggers
intracellular signaling cascades, including tyrosine phosphorylation of
intracellular proteins. We show in this report that p120cbl
(Cbl), the 120-kDa c-cbl proto-oncogene product, becomes
tyrosine-phosphorylated during integrin-mediated macrophage cell
adhesion to extracellular matrix substrata and anti-integrin
antibodies. This tyrosine phosphorylation does not occur when cells
attach to polylysine, to which cells adhere in a nonspecific fashion.
It also does not take place when adhesion-induced reorganization of the
cytoskeleton is inhibited with cytochalasin D. In contrast to the rapid
and transient tyrosine phosphorylation of Cbl by CSF-1 stimulation,
tyrosine phosphorylation of Cbl by cell attachment was gradual and
persistent. Tyrosine-phosphorylated Cbl was found to form complexes
with the SH2 domain-containing signaling proteins Src and
phosphatidylinositol 3-kinase; in vitro kinase assays
demonstrated that these kinases were active in the Cbl complexes
following integrin ligand binding. Furthermore, Cbl was found to
translocate to the plasma membrane in response to cell adhesion to
fibronectin. These observations suggest that Cbl serves as a docking
protein and may transduce signals to downstream signaling pathways
following integrin-mediated cell adhesion in macrophages.
La Jolla Cancer Research Center, The Burnham
Institute, La Jolla, California 92037 and the § Division
of Endocrinology and Metabolism, Department of Medicine, University of
California at San Diego, La Jolla, California 92093
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