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KMID : 0545120140240050714
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Journal of Microbiology and Biotechnology
2014 Volume.24 No. 5 p.714 ~ p.718
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Identification of Novel Binding Partners for Caspase-6 Using a Proteomic Approach
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Jung Ju-Yeon
Lee Su-Rim
Kim Sun-Hong
Chi Seung-Wook
Bae Kwang-Hee
Park Byoung-Chul
Kim Jeong-Hoon
Park Sung-Goo
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Abstract
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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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KEYWORD
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interactome, caspase-6, apoptosis, tandem affinity purification
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