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Identification of Novel Binding Partners for Caspase-6 Using a Proteomic Approach
Identification of Novel Binding Partners for Caspase-6 Using a Proteomic Approach
Journal of Microbiology and Biotechnology. 2014. May, 24(5): 714-718
Copyright © 2014, The Korean Society For Microbiology And Biotechnology
  • Received : December 26, 2013
  • Accepted : February 26, 2014
  • Published : May 28, 2014
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About the Authors
Ju Yeon Jung
Department of Biology, Kongju National University, Kongju 314-701, Republic of Korea
Su Rim Lee
Department of Biology, Kongju National University, Kongju 314-701, Republic of Korea
Sunhong Kim
Targeted Medicine Research Cente
Seung Wook Chi
Medical Proteomics Research Center, Korea Research Institute of Bioscience & Biotechnology, Daejeon 305-333, Republic of Korea
Kwang-Hee Bae
Research Center for Integrative Cellulomics
Byoung Chul Park
Medical Proteomics Research Center, Korea Research Institute of Bioscience & Biotechnology, Daejeon 305-333, Republic of Korea
Jeong-Hoon Kim
Department of Functional Genomics, University of Science and Technology (UST), Daejeon 305-350, Republic of Korea
sgpark@kribb.re.kr
Sung Goo Park
Medical Proteomics Research Center, Korea Research Institute of Bioscience & Biotechnology, Daejeon 305-333, Republic of Korea
sgpark@kribb.re.kr

Abstract
Apoptosis is the process of programmed cell death executed by specific proteases, the caspases, which mediate the cleavage of various vital proteins. Elucidating the consequences of this endoproteolytic cleavage is crucial to understanding cell death and other related biological processes. Although a number of possible roles for caspase-6 have been proposed, the identities and functions of proteins that interact with caspase-6 remain uncertain. In this study, we established a cell line expressing tandem affinity purification (TAP)-tagged caspase-6 and then used LC-MS/MS proteomic analysis to analyze the caspase-6 interactome. Eight candidate caspase-6?interacting proteins were identified. Of these, five proteins (hnRNP-M, DHX38, ASPP2, MTA2, and UACA) were subsequently examined by co-immunoprecipitation for interactions with caspase-6. Thus, we identified two novel members of the caspase-6 interactome: hnRNP-M and MTA2.
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Acknowledgements
This work was supported by KRIBB and research grant from the National Research Foundation of Korea (NRF-2011-0028172).
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