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J Biol Chem, Vol. 274, Issue 6, 3439-3445, February 5, 1999
From the Department of Genetics and Development, College of
Physicians & Surgeons, Columbia University,
New York, New York 10032
Axin is a negative regulator of embryonic
axis formation in vertebrates, which acts through a Wnt signal
transduction pathway involving the serine/threonine kinase GSK-3 and
-catenin. Axin has been shown to have distinct binding sites for
GSK-3 and -catenin and to promote the phosphorylation of -catenin
and its consequent degradation. This provides an explanation for the
ability of Axin to inhibit signaling through -catenin. In addition,
a more N-terminal region of Axin binds to adenomatous polyposis coli
(APC), a tumor suppressor protein that also regulates levels of
-catenin. Here, we report the results of a yeast two-hybrid screen
for proteins that interact with the C-terminal third of Axin, a region
in which no binding sites for other proteins have previously been
identified. We found that Axin can bind to the catalytic subunit of the
serine/threonine protein phosphatase 2A through a domain between amino
acids 632 and 836. This interaction was confirmed by in
vitro binding studies as well as by co-immunoprecipitation of
epitope-tagged proteins expressed in cultured cells. Our results
suggest that protein phosphatase 2A might interact with the
Axin·APC·GSK-3·-catenin complex, where it could modulate the
effect of GSK-3 on -catenin or other proteins in the complex. We
also identified a region of Axin that may allow it to form dimers or
multimers. Through two-hybrid and co-immunoprecipitation studies, we
demonstrated that the C-terminal 100 amino acids of Axin could bind to
the same region as other Axin molecules.
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