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Molecular and Cellular Biology, September 2003, p. 6174-6186, Vol. 23, No. 17
0270-7306/03/$08.00+0     DOI: 10.1128/MCB.23.17.6174-6186.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

ZIP Kinase Triggers Apoptosis from Nuclear PML Oncogenic Domains

Taro Kawai,1 Shizuo Akira,2 and John C. Reed1*

The Burnham Institute, La Jolla, California 92037,1 Department of Host Defense, Research Institute for Microbial Diseases, Osaka University, Osaka, Japan2

Received 10 March 2003/ Returned for modification 15 April 2003/ Accepted 14 May 2003

PML oncogenic domains (PODs), also referred to as nuclear dot 10 bodies, Kreb's bodies, or nuclear bodies, represent nuclear structures implicated in the regulation of a variety of cellular processes, including transcription, tumor suppression, and apoptosis. ZIP kinase (ZIPK) is a proapoptotic protein kinase with homology to DAP kinase, a protein kinase implicated in apoptosis. We show here that ZIPK is present in PODs, where it colocalizes with and binds to proapoptotic protein Daxx. Arsenic trioxide (As2O3) and gamma interferon (IFN-{gamma}), which accentuate POD formation, increased the association of ZIPK with PODs. In contrast, the kinase-inactive ZIPK resides in nuclei with a diffuse pattern and significantly prevents the association of Daxx with PODs, implying that ZIPK recruits Daxx to PODs via its catalytic activity. ZIPK also binds and phosphorylates proapoptotic protein Par-4. Association of ZIPK with Daxx was enhanced by coexpression of Par-4. Activation of caspases and induction of apoptosis were also observed in cells overexpressing these proteins. Conversely, small-interfering RNA-mediated reduction of ZIPK, Daxx, or Par-4 expression decreased activation of caspase and apoptosis induced by As2O3 and IFN-{gamma}. These results suggest that ZIPK, in collaboration with Daxx and Par-4, mediates a novel nuclear pathway for apoptosis.

* Corresponding author. Mailing address: The Burnham Institute, 10901 North Torrey Pines Rd., La Jolla, CA 92037. Phone: (858) 646-3140. Fax: (858) 646-3194. E-mail: reedoffice{at}burnham.org.

Molecular and Cellular Biology, September 2003, p. 6174-6186, Vol. 23, No. 17
0022-538X/03/$08.00+0     DOI: 10.1128/MCB.23.17.6174-6186.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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