Bcl-2 proteins regulate ER membrane permeability to luminal proteins during ER stress-induced apoptosis

@article{Wang2011Bcl2PR,
  title={Bcl-2 proteins regulate ER membrane permeability to luminal proteins during ER stress-induced apoptosis},
  author={X Wang and Kristen E. Olberding and Charlie White and Changqing Li},
  journal={Cell Death and Differentiation},
  year={2011},
  volume={18},
  pages={38-47}
}
Endoplasmic reticulum (ER) stress-induced apoptosis may arise from multiple environmental and pharmacological causes, but the precise mechanism(s) involved are not completely known. Members of Bcl-2 protein family are important regulators of apoptosis. In this study, we report that in a process dependent on the proapoptotic Bcl-2 members Bax and Bak, exogenously expressed fluorescent protein localized to the ER lumen is released into the cytosol in cells undergoing ER stress. Upon ER stress… CONTINUE READING

Citations

Publications citing this paper.
SHOWING 1-10 OF 57 CITATIONS, ESTIMATED 63% COVERAGE

N‐(3‐Oxo‐acyl)‐homoserine lactone induces apoptosis primarily through a mitochondrial pathway in fibroblasts

  • Cellular microbiology
  • 2018
VIEW 9 EXCERPTS
CITES BACKGROUND, METHODS & RESULTS
HIGHLY INFLUENCED

GRP78 at the Centre of the Stage in Cancer and Neuroprotection

  • Front. Neurosci.
  • 2017
VIEW 2 EXCERPTS
CITES BACKGROUND

FILTER CITATIONS BY YEAR

2010
2019

CITATION STATISTICS

  • 3 Highly Influenced Citations

References

Publications referenced by this paper.
SHOWING 1-10 OF 44 REFERENCES

Apoptosis regulation by Bcl-x(L) modulation of mammalian inositol 1,4,5-trisphosphate receptor channel isoform gating.

  • Proceedings of the National Academy of Sciences of the United States of America
  • 2007
VIEW 1 EXCERPT