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AOP-1 Interacts with Cardiac-Specific Protein Kinase TNNI3K and Down-regulates Its Kinase Activity

Yan Feng1, Dong-Qing Liu2, Zhen Wang3, Zhao Liu1, Hui-Qing Cao2, Lai-Yuan Wang2, Na Shi2, and Xian-Min Meng2*

1Department of Pathology, Medical College, Tongji University, 200092 Shanghai, China; fax: +86-21-6598-4636; E-mail: shuangfeiyan888@yahoo.com.cn; ruziliu0486@hotmail.com

2Molecular Medical Center for Cardiovascular Diseases, Fu Wai Cardiovascular Hospital, Peking Union Medical College and Chinese Academy of Medical Sciences, 100037 Beijing, China; fax: +86-10-6831-3012; E-mail: xmmengcn@yahoo.com; liudq1029@yahoo.com

3Department of Pharmacology, School of Basic Medical Sciences, Tongji Medical College, Huazhong University of Science and Technology, 430030 Wuhan, China; E-mail: wzhen2001@sina.com

* To whom correspondence should be addressed.

Received April 2, 2007; Revision received June 4, 2007
In the present study, a yeast two-hybrid screening system was used to identify the interaction partners of cardiac troponin I-interacting kinase (TNNI3K) that might serve as regulators or targets, and thus in turn to gain some insights on the roles of TNNI3K. After screening the adult heart cDNA library with a bait construct encoding the ANK motif of TNNI3K, antioxidant protein 1 (AOP-1) was isolated. The interaction between TNNI3K and AOP-1 was confirmed by the in vitro binding assay and coexpression experiments in vivo. The colocalization of TNNI3K and AOP-1 was clarified by confocal immunofluorescence. Moreover, coexpression of AOP-1 inhibited TNNI3K kinase activity in the in vitro kinase assay.
KEY WORDS: AOP-1, protein kinase, protein-protein interaction, TNNI3K, yeast two-hybrid system

DOI: 10.1134/S0006297907110053