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Biochemistry (Moscow)

, Volume 72, Issue 11, pp 1199–1204 | Cite as

AOP-1 interacts with cardiac-specific protein kinase TNNI3K and down-regulates its kinase activity

  • Yan Feng
  • Dong-Qing Liu
  • Zhen Wang
  • Zhao Liu
  • Hui-Qing Cao
  • Lai-Yuan Wang
  • Na Shi
  • Xian-Min MengEmail author
Article

Abstract

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 

Abbreviations

ANK

ankyrin repeats

AOP-1

antioxidant protein 1

GFP

green fluorescent protein

MBP

myelin basic protein

ROS

reactive oxygen species

TNNI3K

cardiac troponin I-interacting kinase

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Copyright information

© Pleiades Publishing, Ltd. 2007

Authors and Affiliations

  • Yan Feng
    • 1
  • Dong-Qing Liu
    • 2
  • Zhen Wang
    • 3
  • Zhao Liu
    • 1
  • Hui-Qing Cao
    • 2
  • Lai-Yuan Wang
    • 2
  • Na Shi
    • 2
  • Xian-Min Meng
    • 2
    Email author
  1. 1.Department of Pathology, Medical CollegeTongji UniversityShanghaiChina
  2. 2.Molecular Medical Center for Cardiovascular Diseases, Fu Wai Cardiovascular HospitalPeking Union Medical College and Chinese Academy of Medical SciencesBeijingChina
  3. 3.Department of Pharmacology, School of Basic Medical Sciences, Tongji Medical CollegeHuazhong University of Science and TechnologyWuhanChina

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