Cited 3 time in
- Identification of novel binding partners for caspase-6 using a proteomic approach
- Ju Yeon Jung; Su Rim Lee; Sunhong Kim; Seung-Wook Chi; Kwang-Hee Bae; Byoung Chul Park; Jeong Hoon Kim; Sung Goo Park
- Bibliographic Citation
- Journal of Microbiology and Biotechnology, vol. 24, no. 5, pp. 714-718
- Publication Year
- 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.
- ApoptosisCaspase-6InteractomeTandem affinity purification
- Korea Soc-Assoc-Inst
- Appears in Collections:
- Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
Division of Biomedical Research > 1. Journal Articles
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
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