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Molecular and Cellular Biology, August 2004, p. 7188-7196, Vol. 24, No. 16
0270-7306/04/$08.00+0     DOI: 10.1128/MCB.24.16.7188-7196.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Regulation of the Rapsyn Promoter by Kaiso and {delta}-Catenin

Marianna Rodova,1 Kevin F. Kelly,2 Michael VanSaun,1 Juliet M. Daniel,2 and Michael J. Werle1*

Department of Anatomy and Cell Biology, University of Kansas Medical Center, Kansas City, Kansas 66160,1 Department of Biology, McMaster University, Hamilton, Ontario L8S 4K1, Canada2

Received 26 January 2004/ Returned for modification 21 March 2004/ Accepted 20 May 2004

Rapsyn is a synapse-specific protein that is required for clustering acetylcholine receptors at the neuromuscular junction. Analysis of the rapsyn promoter revealed a consensus site for the transcription factor Kaiso within a region that is mutated in a subset of patients with congenital myasthenic syndrome. Kaiso is a POZ-zinc finger family transcription factor which recognizes the specific core consensus sequence CTGCNA (where N is any nucleotide). Previously, the only known binding partner for Kaiso was the cell adhesion cofactor, p120 catenin. Here we show that {delta}-catenin, a brain-specific member of the p120 catenin subfamily, forms a complex with Kaiso. Antibodies against Kaiso and {delta}-catenin recognize proteins in the nuclei of C2C12 myocytes and at the postsynaptic domain of the mouse neuromuscular junction. Endogenous Kaiso in C2C12 cells coprecipitates with the rapsyn promoter in vivo as shown by chromatin immunoprecipitation assay. Minimal promoter assays demonstrated that the rapsyn promoter can be activated by Kaiso and {delta}-catenin; this activation is apparently muscle specific. These results provide the first experimental evidence that rapsyn is a direct sequence-specific target of Kaiso and {delta}-catenin. We propose a new model of synapse-specific transcription that involves the interaction of Kaiso, {delta}-catenin, and myogenic transcription factors at the neuromuscular junction.

* Corresponding author. Mailing address: Department of Anatomy and Cell Biology, Mail Stop 3038, University of Kansas Medical Center, 3901 Rainbow Blvd., Kansas City, KS 66160-7421. Phone: (913) 588-7491. Fax: (913) 588-2710. E-mail: mwerle{at}kumc.edu.

Molecular and Cellular Biology, August 2004, p. 7188-7196, Vol. 24, No. 16
0022-538X/04/$08.00+0     DOI: 10.1128/MCB.24.16.7188-7196.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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