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J Biol Chem, Vol. 273, Issue 18, 10823-10826, May 1, 1998
-Catenin
From the Department of Biochemistry, Hiroshima University School of
Medicine, 1-2-3 Kasumi, Minami-ku, Hiroshima 734-8551, Japan
The regulators of G protein signaling (RGS)
domain of Axin, a negative regulator of the Wnt signaling pathway, made
a complex with full-length adenomatous polyposis coli (APC) in COS,
293, and L cells but not with truncated APC in SW480 or DLD-1 cells. The RGS domain directly interacted with the region containing the
20-amino acid repeats but not with that containing the 15-amino acid
repeats of APC, although both regions are known to bind to 
-catenin.
In the region containing seven 20-amino acid repeats, the region
containing the latter five repeats bound to the RGS domain of Axin.
Axin and -catenin simultaneously interacted with APC. Furthermore,
Axin stimulated the degradation of -catenin in COS cells. Taken
together with our recent observations that Axin directly interacts with
glycogen synthase kinase-3 (GSK-3) and -catenin and that it
promotes GSK-3-dependent phosphorylation of -catenin,
these results suggest that Axin, APC, GSK-3, and -catenin make a
tetrameric complex, resulting in the regulation of the stabilization of
-catenin.
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