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Anti‐apoptotic activity of Bcl‐2 is enhanced by its interaction with RTN3
Author(s) -
Zhu Lei,
Xiang Rong,
Dong Wei,
Liu Yingle,
Qi Yipeng
Publication year - 2007
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1016/j.cellbi.2007.01.032
Subject(s) - hela , microbiology and biotechnology , endoplasmic reticulum , apoptosis , mitochondrion , cytoplasm , bcl 2 family , tunicamycin , chemistry , ectopic expression , mitochondrial apoptosis induced channel , microsome , biology , cell , cell culture , programmed cell death , unfolded protein response , biochemistry , inner mitochondrial membrane , in vitro , genetics
Bcl‐2 is known as a critical inhibitor of apoptosis triggered by a broad range of stimuli, mainly acting on the mitochondria. It can interact with many members of the Bcl‐2 family, influence mitochondrial membrane permeability and modulate cell apoptosis. RTN3, a member of the reticulon (RTN) family, was predominantly localized on the endoplasmic reticulum (ER). Its N‐ and C‐termini, both facing the cytoplasm, can recruit some proteins to the ER to modulate some physiological functions. We found that RTN3, which does not belong to the Bcl‐2 family, can interact with Bcl‐2 on the ER. In normal HeLa cells, ectopic overexpressed Bcl‐2 could reduce the cell apoptosis induced by overexpressed RTN3. When the HeLa cells stably expressing Bcl‐2 were treated with tunicamycin, endogenous RTN3 increased in the cell microsomal fraction. This change increased the Bcl‐2 in microsomal fractions and also in the mitochondrial fractions where the anti‐apoptotic activity of Bcl‐2 mainly acts. These results suggest that RTN3 could bind with Bcl‐2 and mediate its accumulation in mitochondria, which modulate the anti‐apoptotic activity of Bcl‐2.