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

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dc.contributor.authorJu Yeon Jung-
dc.contributor.authorSu Rim Lee-
dc.contributor.authorSunhong Kim-
dc.contributor.authorSeung-Wook Chi-
dc.contributor.authorKwang-Hee Bae-
dc.contributor.authorByoung Chul Park-
dc.contributor.authorJeong Hoon Kim-
dc.contributor.authorSung Goo Park-
dc.date.accessioned2017-04-19T09:53:13Z-
dc.date.available2017-04-19T09:53:13Z-
dc.date.issued2014-
dc.identifier.issn1017-7825-
dc.identifier.uri10.4014/jmb.1312.12068ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/11992-
dc.description.abstractApoptosis 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.-
dc.publisherKorea Soc-Assoc-Inst-
dc.titleIdentification of novel binding partners for caspase-6 using a proteomic approach-
dc.title.alternativeIdentification of novel binding partners for caspase-6 using a proteomic approach-
dc.typeArticle-
dc.citation.titleJournal of Microbiology and Biotechnology-
dc.citation.number5-
dc.citation.endPage718-
dc.citation.startPage714-
dc.citation.volume24-
dc.contributor.affiliatedAuthorJu Yeon Jung-
dc.contributor.affiliatedAuthorSu Rim Lee-
dc.contributor.affiliatedAuthorSunhong Kim-
dc.contributor.affiliatedAuthorSeung-Wook Chi-
dc.contributor.affiliatedAuthorKwang-Hee Bae-
dc.contributor.affiliatedAuthorByoung Chul Park-
dc.contributor.affiliatedAuthorJeong Hoon Kim-
dc.contributor.affiliatedAuthorSung Goo Park-
dc.contributor.alternativeName정주연-
dc.contributor.alternativeName이수림-
dc.contributor.alternativeName김선홍-
dc.contributor.alternativeName지승욱-
dc.contributor.alternativeName배광희-
dc.contributor.alternativeName박병철-
dc.contributor.alternativeName김정훈-
dc.contributor.alternativeName박성구-
dc.identifier.bibliographicCitationJournal of Microbiology and Biotechnology, vol. 24, no. 5, pp. 714-718-
dc.identifier.doi10.4014/jmb.1312.12068-
dc.subject.keywordApoptosis-
dc.subject.keywordCaspase-6-
dc.subject.keywordInteractome-
dc.subject.keywordTandem affinity purification-
dc.subject.localapoptosis-
dc.subject.localApoptosis-
dc.subject.localCaspase-6-
dc.subject.localInteractome-
dc.subject.localinteractome-
dc.subject.localTandem affinity purification-
dc.description.journalClassY-
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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