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Title 

Apoptosis-linked gene 2 binds to the death domain of fas and dissociates from fas during fas-mediated apoptosis in jurkat cells

Authors 

Yong Sam JungKeun Soo KimKwang Dong KimJong-Seok LimJung Woo KimEun Hee Kim

Publisher 

Elsevier

Issue Date 

2001

Citation 

Biochemical and Biophysical Research Communications, vol. 288, no. 2, pp. 420-426

Keywords 

ALG-2FasJurkat cellapoptosisbindingcleavagetranslocation

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 Fasmediated 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.

ISSN 

0006-291X

Link 

http://dx.doi.org/10.1006/bbrc.2001.5769

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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