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J. Biol. Chem., Vol. 276, Issue 9, 6061-6064, March 2, 2001
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and -Catenin*
From the Dana-Farber Cancer Institute, Harvard Medical School,
Boston, Massachusetts 02115
The DF3/MUC1 mucin-like glycoprotein is
aberrantly overexpressed in most human carcinomas. The cytoplasmic
domain of MUC1 interacts with glycogen synthase kinase 3
(GSK3)
and thereby decreases binding of MUC1 and -catenin. The present
studies demonstrate that MUC1 associates with the c-Src tyrosine
kinase. c-Src phosphorylates the MUC1 cytoplasmic domain at a YEKV
motif located between sites involved in interactions with GSK3 and
-catenin. The results demonstrate that the c-Src SH2 domain binds
directly to pYEKV and inhibits the interaction between MUC1 and
GSK3. Moreover and in contrast to GSK3, in vitro and
in vivo studies demonstrate that c-Src-mediated
phosphorylation of MUC1 increases binding of MUC1 and -catenin.
The findings support a novel role for c-Src in regulating
interactions of MUC1 with GSK3 and -catenin.
To whom correspondence should be addressed. Tel.: 617-632-3141;
Fax: 617-632-2934; E-mail: donald_kufe@dfci.harvard.edu.
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