The modification and assembly of proteins in the endoplasmic reticulum

https://doi.org/10.1016/0955-0674(93)90127-CGet rights and content

Abstract

Proteins fold and assemble in the endoplasmic reticulum in an environment that is very different from the cytosol. The presence of relatively high concentrations of calcium, an oxidizing state, ATP and lumenal proteins are all important in mediating these events.

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      Disturbed ER homeostasis induces ER stress, characterized by Ca2+ release from ER into cytoplasm and a surge of unfolded or misfolded proteins (Bukau et al., 2006; Gaut and Hendershot, 1993). This in turn leads to increased expression of ER chaperon proteins to restore ER homeostasis (Bukau et al., 2006; Gaut and Hendershot, 1993). Increased cytosolic Ca2+ may disturb Ca2+ signaling, upregulate mitochondrial Ca2+ load, and trigger cell death (Bukau et al., 2006; Gaut and Hendershot, 1993; Rizzuto et al., 1998).

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