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Mol Cell Biol, March 1998, p. 1642-1651, Vol. 18, No. 3
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

ZIP Kinase, a Novel Serine/Threonine Kinase Which Mediates Apoptosis

Taro Kawai, Makoto Matsumoto, Kiyoshi Takeda, Hideki Sanjo, and Shizuo Akira*

Department of Biochemistry, Hyogo College of Medicine, Nishinomiya, Hyogo 663, Japan

Received 25 September 1997/Returned for modification 30 October 1997/Accepted 11 December 1997

We have identified a novel serine/threonine kinase, designated ZIP kinase, which mediates apoptosis. ZIP kinase contains a leucine zipper structure at its C terminus, in addition to a kinase domain at its N terminus. ZIP kinase physically binds to ATF4, a member of the activating transcription factor/cyclic AMP-responsive element-binding protein (ATF/CREB) family, through interaction between their leucine zippers. The leucine zipper domain is necessary for the homodimerization of ZIP kinase as well as for the activation of kinase. Immunostaining study showed that ZIP kinase localizes in the nuclei. Overexpression of intact ZIP kinase but not catalytically inactive kinase mutants led to the morphological changes of apoptosis in NIH 3T3 cells, suggesting that the cell death-inducing activity of ZIP kinase depends on its intrinsic kinase activity. Interestingly, the catalytic domain of ZIP kinase is closely related to that of death-associated protein kinase (DAP kinase), which is a mediator of apoptosis induced by gamma interferon. Therefore, both ZIP and DAP kinases represent a novel kinase family, which mediates apoptosis through their catalytic activities.

* Corresponding author. Mailing address: Department of Biochemistry, Hyogo College of Medicine, 1-1 Mukogawa-cho, Nishinomiya, Hyogo 663, Japan. Phone: 81-798-45-6357. Fax: 81-798-46-3164. E-mail: akira{at}hyo-med.ac.jp.




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