Journal
CELL DEATH AND DIFFERENTIATION
Volume 11, Issue 4, Pages 372-380Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/sj.cdd.4401378
Keywords
endoplasmic reticulum; ER stress; caspase; misfolded proteins; apoptosis; apostat
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Funding
- NCI NIH HHS [CA84262] Funding Source: Medline
- NIA NIH HHS [AG12282] Funding Source: Medline
- NINDS NIH HHS [NS33376] Funding Source: Medline
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The endoplasmic reticulum ( ER) regulates protein synthesis, protein folding and trafficking, cellular responses to stress and intracellular calcium (Ca2+) levels. Alterations in Ca2+ homeostasis and accumulation of misfolded proteins in the ER cause ER stress that ultimately leads to apoptosis. Prolonged ER stress is linked to the pathogenesis of several different neurodegenerative disorders. Apoptosis is a form of cell death that involves the concerted action of a number of intracellular signaling pathways including members of the caspase family of cysteine proteases. The two main apoptotic pathways, the death receptor ('extrinsic') and mitochondrial ('intrinsic') pathways, are activated by caspase-8 and - 9, respectively, both of which are found in the cytoplasm. Recent studies point to the ER as a third subcellular compartment implicated in apoptotic execution. Here, we review evidence for the contribution of various cellular molecules that contribute to ER stress and subsequent cellular death. It is hoped that dissection of the molecular components and pathways that alter ER structure and function and ultimately promote cellular death will provide a framework for understanding degenerative disorders that feature misfolded proteins.
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