Apoptosis-linked gene 2 binds to the death domain of Fas and dissociates from Fas during Fas-mediated apoptosis in Jurkat cells
DC Field | Value | Language |
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dc.contributor.author | Jung, YS | - |
dc.contributor.author | Kim, KS | - |
dc.contributor.author | Kim, KD | - |
dc.contributor.author | Lim, JS | - |
dc.contributor.author | Kim, JW | - |
dc.contributor.author | Kim, E | - |
dc.date.accessioned | 2022-04-19T12:43:01Z | - |
dc.date.available | 2022-04-19T12:43:01Z | - |
dc.date.issued | 2001-10 | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.issn | 1090-2104 | - |
dc.identifier.uri | https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/149691 | - |
dc.description.abstract | Apoptosis-linked gene 2 (ALG-2) is a member of the family of Ca2+-binding proteins with penta-EF-hand and is essential for the execution of apoptosis by various signals including Fas activation. We studied the regulation of ALG-2 during Fas-mediated apoptosis in Jurkat cells. The 22-kDa ALG-2 protein is cleaved and becomes a 19-kDa protein after Fas activation. The appearance of 19-kDa ALG-2 protein increases for 4 h after treatment with 200 ng/ml of anti-Fas Ab treatment and gradually degrades afterward. Confocal microscopic analysis showed that ALG-2 translocated from the plasma membrane to the cytosol during Fas-mediated apoptosis. Therefore, we examined if ALG-2 interacts with Fas. The protein-protein interaction of ALG-2 with Fas was demonstrated using yeast two-hybrid assays as well as in vitro GST pull-down assay. Endogenous ALG-2 was immunoprecipitated with anti-Fas Ab in Jurkat cells without Fas activation. However, the endogenous ALG-2 was no longer immunoprecipitated with anti-Fas Ab 2 h after anti-Fas Ab treatment. This study, for the first time, presents a direct molecular connection of ALG-2 to apoptosis by its direct interaction with Fas, and enlists ALG-2 as a new member of posttranslationally modified proteins during Fas-mediated apoptotic process. (C) 2001 Academic Press. | - |
dc.format.extent | 7 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | ACADEMIC PRESS INC ELSEVIER SCIENCE | - |
dc.title | Apoptosis-linked gene 2 binds to the death domain of Fas and dissociates from Fas during Fas-mediated apoptosis in Jurkat cells | - |
dc.type | Article | - |
dc.publisher.location | 미국 | - |
dc.identifier.doi | 10.1006/bbrc.2001.5769 | - |
dc.identifier.scopusid | 2-s2.0-0035955332 | - |
dc.identifier.wosid | 000171961900019 | - |
dc.identifier.bibliographicCitation | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.288, no.2, pp 420 - 426 | - |
dc.citation.title | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.citation.volume | 288 | - |
dc.citation.number | 2 | - |
dc.citation.startPage | 420 | - |
dc.citation.endPage | 426 | - |
dc.description.isOpenAccess | N | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.subject.keywordPlus | PROTEIN ALG-2 | - |
dc.subject.keywordPlus | SMALL-SUBUNIT | - |
dc.subject.keywordPlus | ACTIVATION | - |
dc.subject.keywordPlus | FAMILY | - |
dc.subject.keywordPlus | MEMBER | - |
dc.subject.keywordPlus | BAX | - |
dc.subject.keywordPlus | EXPRESSION | - |
dc.subject.keywordPlus | PROTEASES | - |
dc.subject.keywordPlus | CASPASES | - |
dc.subject.keywordPlus | CLEAVAGE | - |
dc.subject.keywordAuthor | ALG-2 | - |
dc.subject.keywordAuthor | Fas | - |
dc.subject.keywordAuthor | Jurkat cell | - |
dc.subject.keywordAuthor | apoptosis | - |
dc.subject.keywordAuthor | binding | - |
dc.subject.keywordAuthor | cleavage | - |
dc.subject.keywordAuthor | translocation | - |
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