Apoptosis-linked gene 2 binds to the death domain of Fas and dissociates from Fas during Fas-mediated apoptosis in Jurkat cells
- Authors
- Jung, YS; Kim, KS; Kim, KD; Lim, JS; Kim, JW; Kim, E
- Issue Date
- Oct-2001
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- Keywords
- ALG-2; Fas; Jurkat cell; apoptosis; binding; cleavage; translocation
- Citation
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.288, no.2, pp 420 - 426
- Pages
- 7
- Journal Title
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- Volume
- 288
- Number
- 2
- Start Page
- 420
- End Page
- 426
- URI
- https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/149691
- DOI
- 10.1006/bbrc.2001.5769
- ISSN
- 0006-291X
1090-2104
- 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.
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