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Vol. 12, No. 10, pp. 1425-1437, May 15, 1998
1 Yale University School of Medicine, Department of
Genetics, New Haven, Connecticut 06520-8005 USA;
2 Howard
Hughes Medical Institute, Department of Biology, Massachusetts
Institute of Technology, Cambridge, Massachusetts 02139 USA
Receptor tyrosine phosphatases have been implicated in playing
important roles in cell signaling events by their ability to regulate
the level of protein tyrosine phosphorylation. Although the catalytic
activity of their phosphatase domains has been well established, the
biological roles of these molecules are, for the most part, not well
understood. Here we show that the Caenorhabditis elegans
protein CLR-1 (CLeaR) is a receptor tyrosine phosphatase (RTP) with a
complex extracellular region and two intracellular phosphatase domains.
Mutations in clr-1 result in a dramatic Clr phenotype that we
have used to study the physiological requirements for the CLR-1 RTP. We
show that the phosphatase activity of the membrane-proximal domain is
essential for the in vivo function of CLR-1. By contrast, we present
evidence that the membrane-distal domain is not required to prevent the
Clr phenotype in vivo. The Clr phenotype of clr-1 mutants is
mimicked by activation of the EGL-15 fibroblast growth factor receptor
(FGFR) and is suppressed by mutations that reduce or eliminate the
activity of egl-15. Our data strongly indicate that CLR-1
attenuates the action of an FGFR-mediated signaling pathway by
dephosphorylation.
[Key Words: FGF receptor tyrosine kinase; tyrosine phosphatase; C. elegans; CLR-1; EGL-15]
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