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Molecular and Cellular Biology, December 2006, p. 8857-8867, Vol. 26, No. 23
0270-7306/06/$08.00+0     doi:10.1128/MCB.01031-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

LZTS2 Is a Novel ß-Catenin-Interacting Protein and Regulates the Nuclear Export of ß-Catenin{triangledown}

Gregory Thyssen, Tzu-Huey Li, Lynn Lehmann, Ming Zhuo, Manju Sharma, and Zijie Sun*

Departments of Urology and Genetics, Stanford University School of Medicine, Stanford, California 94305-5118

Received 8 June 2006/ Returned for modification 19 June 2006/ Accepted 30 August 2006

ß-Catenin plays multiple roles in cell-cell adhesion and Wnt signal transduction. Through the Wnt signal, the cellular level of ß-catenin is constitutively regulated by the multicomponent destruction complex containing glycogen synthase kinase 3ß, axin, and adenomatous polyposis coli. Here, we present multiple lines of evidence to demonstrate that LZTS2 (lucine zipper tumor suppressor 2) interacts with ß-catenin, represses the transactivation of ß-catenin, and affects the subcellular localization of ß-catenin. The LZTS2 gene is located at 10q24.3, which is frequently lost in a variety of human tumors. A functional nuclear export signal (NES) was identified in the C terminus of the protein (amino acids 631 to 641). Appending this motif to green fluorescent protein (GFP) induced nuclear exclusion of the GFP fusion protein. However, introducing point mutations in either one or two leucine residues of this NES sequence abolished the nuclear exclusion of the LZTS2 protein. The nuclear export of LZTS2 can be blocked by leptomycin B (LMB), an inhibitor of the CRM1/exportin-alpha pathway. Intriguingly, ß-catenin colocalizes with LZTS2 in the cytoplasm of cells in the absence of LMB but in the nuclei of cells in the presence of LMB. Increasing the LZTS2 protein in cells reduces the level of nuclear ß-catenin in SW480 cells. Taken together, these data demonstrate that LZTS2 is a ß-catenin-interacting protein that can modulate ß-catenin signaling and localization.

* Corresponding author. Mailing address: Departments of Urology and Genetics, 300 Pasteur Drive, Grant Bldg. S287, Stanford University School of Medicine, Stanford, CA 94305-5118. Phone: (650) 498-7523. Fax: (650) 723-4200. E-mail: zsun{at}stanford.edu.

{triangledown} Published ahead of print on 25 September 2006.

Molecular and Cellular Biology, December 2006, p. 8857-8867, Vol. 26, No. 23
0270-7306/06/$08.00+0     doi:10.1128/MCB.01031-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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