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CPEB4 links the clock and the UPR to protect the liver

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Under misfolded protein stress, the endoplasmic reticulum (ER) activates the unfolded protein response (UPR) to restore homeostasis, or commits the cell to apoptosis. A study now uncovers how the UPR is governed by the circadian clock to adjust ER protein-folding capacity to metabolic demand and protect against liver damage.

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Figure 1: Rhythmic transcription and UPR-mediated translation of Cpeb4 synchronize to protect hepatocytes against metabolic demand.

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Authors and Affiliations

  1. Paul C. Moore and Scott A. Oakes are in the Department of Pathology, Diabetes Center, and Helen Diller Family Comprehensive Cancer Center at the University of California, San Francisco, California 94143, USA,

    Paul C. Moore & Scott A. Oakes

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  1. Paul C. Moore
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  2. Scott A. Oakes
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Correspondence to Scott A. Oakes.

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Competing interests

S.A.O. is a founder, equity holder, and consultant for OptiKira, L.L.C. (Cleveland, Ohio).

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Moore, P., Oakes, S. CPEB4 links the clock and the UPR to protect the liver. Nat Cell Biol 19, 79–81 (2017). https://doi.org/10.1038/ncb3460

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