Identification of novel binding partners for caspase-6 using a proteomic approach

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Title
Identification of novel binding partners for caspase-6 using a proteomic approach
Author(s)
Ju Yeon Jung; Su Rim Lee; Sunhong Kim; Seung-Wook ChiKwang-Hee BaeByoung Chul ParkJeong Hoon KimSung Goo Park
Bibliographic Citation
Journal of Microbiology and Biotechnology, vol. 24, no. 5, pp. 714-718
Publication Year
2014
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.
Keyword
ApoptosisCaspase-6InteractomeTandem affinity purification
ISSN
1017-7825
Publisher
Korea Soc-Assoc-Inst
DOI
http://dx.doi.org/10.4014/jmb.1312.12068
Type
Article
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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