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Protein folding homeostasis in the endoplasmic reticulum: tuning a chaperone

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A transcriptional and translational program that strives to match the complement of chaperones in the endoplasmic reticulum (ER) to the burden of unfolded proteins in the early secretory pathway (the Unfolded Protein Response) has long been known to exist and its functional importance has been showcased by genetic and pharmacological manipulations. However, theoretical considerations supported by experimental observations highlight the latency inherent in this gene expression program and suggest the potential importance of post-translational adaptations that operate on a shorter time scale. This seminar will review some recent observations pertaining to an ER-localized circuitry that tunes the activity of the compartment’s resident Hsp70 protein, BiP, to rapid fluctuations in unfolded protein load.

This talk is part of the MRC LMB Seminar Series series.

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