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J. Biol. Chem., Vol. 278, Issue 15, 13265-13270, April 11, 2003
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From the The Trio guanine nucleotide exchange factor
functions in neural development in Caenorhabditis elegans
and Drosophila and in the development of neural tissues and
skeletal muscle in mouse. The association of Trio with the Lar tyrosine
phosphatase led us to study the role of tyrosine phosphorylation in
Trio function using focal adhesion kinase (FAK). The Lar-interacting
domain of Trio is constitutively tyrosine-phosphorylated when expressed in COS-7 cells and was highly phosphorylated when it was co-transfected with FAK. Co-precipitation studies indicated that Trio binds to the FAK
amino-terminal domain and to the FAK kinase domain via its SH3 and
kinase domains, respectively. Tyrosine-phosphorylated FAK and Trio were
present mainly in the detergent-insoluble fraction of cell lysates, and
co-expression of Trio and FAK resulted in increased amounts of Trio
present in the detergent-insoluble fraction. Immunofluorescence of
cells co-transfected with FAK and Trio revealed significant
co-localization of the proteins at the cell periphery, indicating that
they form a stable complex in vivo. A FAK phosphorylation site, tyrosine residue 2737, was identified in subdomain I of the Trio
kinase domain. Additionally, in vitro phosphorylation assays and in vivo co-expression studies indicated that
Trio enhances FAK kinase activity. These results suggest Trio may be
involved in the regulation of focal adhesion dynamics in addition to
effecting changes in the actin cytoskeleton through the activation of
Rho family GTPases.
Signaling between Focal Adhesion Kinase and
Trio*
§¶,,
,,, and§
Department of Cancer Immunology and AIDS,
Dana-Farber Cancer Institute, Boston, Massachusetts 02115 and the
Departments of § Pathology and Medicine, Harvard
Medical School, Boston, Massachusetts 02115
*
This work was supported by Grants CA55547 and CA75091 from
the National Institutes of Health and a Medical Research Council of
Canada Fellowship (to Q. G. M.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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