These authors contributed equally to this work.
Anti-apoptotic activity of Bcl-2 is enhanced by its interaction with RTN3
Version of Record online: 2 JAN 2013
© The Author(s) Journal compilation © 2007 International Federation for Cell Biology
Cell Biology International
Volume 31, Issue 8, pages 825–830, August 2007
How to Cite
Zhu, L., Xiang, R., Dong, W., Liu, Y. and Qi, Y. (2007), Anti-apoptotic activity of Bcl-2 is enhanced by its interaction with RTN3. Cell Biology International, 31: 825–830. doi: 10.1016/j.cellbi.2007.01.032
- Issue online: 2 JAN 2013
- Version of Record online: 2 JAN 2013
- Received 20 November 2006; revised 28 December 2006; accepted 18 January 2007
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.