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Originally published In Press as doi:10.1074/jbc.M109508200 on December 19, 2001
J. Biol. Chem., Vol. 277, Issue 10, 8202-8208, March 8, 2002
Isolation and Characterization of XKaiso, a Transcriptional
Repressor That Associates with the Catenin Xp120ctn in
Xenopus laevis*
Si Wan
Kim ,
Xiang
Fang ,
Hong
Ji ,
Alicia F.
Paulson ,
Juliet M.
Daniel§,
Malgorzata
Ciesiolka¶,
Frans
van
Roy¶, and
Pierre D.
McCrea **
From the Department of Biochemistry and Molecular
Biology, Program in Genes and Development, The University of
Texas M.D. Anderson Cancer Center, Houston, Texas 77030, the
§ Department of Biology, McMaster University, Hamilton,
Ontario L8S 4K1, Canada, and the ¶ Department of Molecular
Biology, VIB-University of Gent, Ledeganckstraat 35, B-9000 Gent, Belgium
The Armadillo family of catenin proteins function
in multiple capacities including cadherin-mediated cell-cell adhesion
and nuclear signaling. The newest catenin, p120ctn,
differs from the classical catenins and binds to the membrane-proximal domain of cadherins. Recently, a novel transcription factor Kaiso was
found to interact with p120ctn, suggesting that p120ctn
also possesses a nuclear function. We isolated the Xenopus
homolog of Kaiso, XKaiso, from a Xenopus stage 17 cDNA
library. XKaiso contains an amino-terminal BTB/POZ domain and three
carboxyl-terminal zinc fingers. The XKaiso transcript was present
maternally and expressed throughout early embryonic development.
XKaiso's spatial expression was defined via in situ
hybridization and was found localized to the brain, eye, ear, branchial
arches, and spinal cord. Co-immunoprecipitation of Xenopus
p120ctn and XKaiso demonstrated their mutual association,
whereas related experiments employing differentially epitope-tagged
XKaiso constructs suggest that XKaiso additionally self-associates.
Finally, reporter assays employing a chimera of XKaiso fused to the
GAL4 DNA binding domain indicate that XKaiso is a transcriptional
repressor. These data suggest that XKaiso functions throughout
development and that its repressor functions may be most apparent in
the context of neural tissues. The significance of the
XKaiso-p120ctn interaction has yet to be determined, but it may
include transducing information from cadherin-mediated cell-cell
contacts to transcriptional processes within the nucleus.
*
This work was supported in part by National Institutes of
Health RO1 Grant GM 52112, a Pharmacia/Monsanto Research Award, a
Kleberg Foundation Award, and Cancer Center Support Grant Funds CCSG-CA
16672 (to P. D. M.) and by the Fund for Scientific Research-Flanders and Fortis Verzekeringen (Belgium) (to F. V. R.).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.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AF420316.
**
To whom correspondence should be addressed: Dept. of Biochemistry
and Molecular Biology, Box 117, The University of Texas M.D. Anderson
Cancer Center, 1515 Holcombe Blvd., Houston, TX 77030. Tel.:
713-792-8979; Fax: 713-791-9478; E-mail:
pmccrea@odin.mdacc.tmc.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 2002 by the American Society for Biochemistry and Molecular Biology.
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