The deadly connection between endoplasmic reticulum, Ca2+, protein synthesis, and the endoplasmic reticulum stress response in malignant glioma cells
Author(s) -
Guyla G. Johnson,
Misti C. White,
Jian-He Wu,
Matthew Vallejo,
M. Grimaldi
Publication year - 2014
Publication title -
neuro-oncology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.005
H-Index - 125
eISSN - 1523-5866
pISSN - 1522-8517
DOI - 10.1093/neuonc/nou012
Subject(s) - unfolded protein response , endoplasmic reticulum , glioma , microbiology and biotechnology , translocon , programmed cell death , biology , stim1 , cancer research , chemistry , apoptosis , biochemistry , membrane protein , membrane
The endoplasmic reticulum (ER) is involved in Ca(2+) signaling and protein processing. Accumulation of unfolded proteins following ER Ca(2+) depletion triggers the ER stress response (ERSR), which facilitates protein folding and removal of damaged proteins and can induce cell death. Unfolded proteins bind to chaperones, such as the glucose-regulated protein (GRP)78 and cause the release of GRP78-repressed proteins executing ERSR.
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