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Title 

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

Authors 

Ju Yeon JungSu Rim LeeSunhong KimSeung-Wook ChiKwang-Hee BaeByoung Chul ParkJeong Hoon KimSung Goo Park

Publisher 

The Korean Society for Applied Microbiology

Issue Date 

2014

Citation 

Journal of Microbiology and Biotechnology, vol. 24, no. 5, pp. 714-718

Keywords 

ApoptosisCaspase-6InteractomeTandem affinity purification

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.

ISSN 

1017-7825

Link 

http://dx.doi.org/10.4014/jmb.1312.12068

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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