Abstract
Maintenance of protein homeostasis depends on cellular stress
response pathways that mediate adaptive changes in gene expression.In the endoplasmic reticulum additional mechanisms adjust the availability of the abundant Hsp70-type chaperone, BiP, during short-term
fluctuations in the unfolded protein load. Here, recent insights into theregulation of BiP by incorporation into inactive oligomers and reversible AMPylation are discussed.
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