DOI QR코드

DOI QR Code

Identification of Novel Binding Partners for Caspase-6 Using a Proteomic Approach

  • Jung, Ju Yeon (Medical Proteomics Research Center, Korea Research Institute of Bioscience & Biotechnology) ;
  • Lee, Su Rim (Medical Proteomics Research Center, Korea Research Institute of Bioscience & Biotechnology) ;
  • Kim, Sunhong (Targeted Medicine Research Center, Korea Research Institute of Bioscience & Biotechnology) ;
  • Chi, Seung Wook (Medical Proteomics Research Center, Korea Research Institute of Bioscience & Biotechnology) ;
  • Bae, Kwang-Hee (Research Center for Integrative Cellulomics, Korea Research Institute of Bioscience & Biotechnology) ;
  • Park, Byoung Chul (Medical Proteomics Research Center, Korea Research Institute of Bioscience & Biotechnology) ;
  • Kim, Jeong-Hoon (Targeted Gene Regulation Research Center, Korea Research Institute of Bioscience & Biotechnology) ;
  • Park, Sung Goo (Medical Proteomics Research Center, Korea Research Institute of Bioscience & Biotechnology)
  • 투고 : 2013.12.26
  • 심사 : 2014.02.26
  • 발행 : 2014.05.28

초록

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.

키워드

참고문헌

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