Regulation of chaperone activity in the endoplasmic reticulum

Abstract

<jats:title>Abstract</jats:title><jats:p>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 the regulation of BiP by incorporation into inactive oligomers and reversible AMPylation are discussed.</jats:p>