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J. Biol. Chem., Vol. 278, Issue 8, 5728-5735, February 21, 2003
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From the The receptor protein-tyrosine phosphatase (PTP)
DEP-1 (CD148/PTP-
Hepatocyte Growth Factor Receptor Tyrosine Kinase Met Is a
Substrate of the Receptor Protein-tyrosine Phosphatase DEP-1*
§,
Cold Spring Harbor Laboratory, Cold Spring
Harbor, New York 11724 and the ¶ Molecular Oncology Group, McGill
University Hospital Center, Montreal, Quebec H3A 1A1, Canada
) has been implicated in the regulation of cell
growth, differentiation, and transformation, and most recently has been identified as a potential tumor suppressor gene mutated in colon, lung,
and breast cancers. We have generated constructs comprising the
cytoplasmic segment of DEP-1 fused to the maltose-binding protein to
identify potential substrates and thereby suggest a physiological
function for DEP-1. We have shown that the substrate-trapping mutant
form of DEP-1 interacted with a small subset of tyrosine-phosphorylated proteins from lysates of the human breast tumor cell lines MDA-MB-231, T-47D, and T-47D/Met and have identified the hepatocyte growth factor/scatter factor receptor Met, the adapter protein Gab1, and the junctional component p120 catenin as potential substrates. Following ligand stimulation, phosphorylation of specific tyrosyl residues in Met induces mitogenic, motogenic, and morphogenic responses. When co-expressed in 293 cells, the full-length
substrate-trapping mutant form of DEP-1 formed a stable complex with
the chimeric receptor colony stimulating factor 1 (CSF)-Met and
wild type DEP-1 dephosphorylated CSF-Met. Furthermore, we observed that
DEP-1 preferentially dephosphorylated a Gab1 binding site
(Tyr1349) and a COOH-terminal tyrosine implicated in
morphogenesis (Tyr1365), whereas tyrosine residues in the
activation loop of Met (Tyr1230, Tyr1234, and
Tyr1235) were not preferred targets of the PTP. The ability
of DEP-1 preferentially to dephosphorylate particular tyrosine residues that are required for Met-induced signaling suggests that DEP-1 may
function in controlling the specificity of signals induced by this PTK,
rather than as a simple "off-switch" to counteract PTK activity.
*
This work was supported in part by National Institutes of
Health Grant RO1-GM55989 (to N. K. T.).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.
To whom correspondence should be addressed: Cold Spring Harbor
Laboratory, Cold Spring Harbor, NY 11724. Tel.: 516-367-8846; Fax:
516-367-6812; E-mail: tonks@cshl.org.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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