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Cell biology

The TORC1 pathway to protein destruction

Nature volume 536, pages 155–156 (2016)Cite this article

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A study of the proteasome — a protein-degradation complex — reveals an evolutionarily conserved pathway that acts through the protein kinase TORC1 to adjust proteasome levels in response to cellular needs. See Letter p.184

To maintain amino-acid and protein levels, cells must couple nutrient availability to protein synthesis and turnover. Central to this process is the enzyme called target of rapamycin complex 1 (TORC1) kinase, a master growth controller that integrates diverse environmental inputs to coordinate many metabolic processes1. Rousseau and Bertolotti2 reveal on page 184 that inhibition of TORC1 increases levels of the proteasome — a large protein complex involved in cellular protein degradation — to promote cell survival under stressful conditions. Consistent with previous reports3,4,5, the new work identifies TORC1 as a central regulator of proteasome homeostasis. However, the relationship between TORC1 and the control of proteasome function seems to be complex, because TORC1 can regulate the proteasome through multiple mechanisms that depend on the particular cellular context3,4,5.

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Figure 1: Evolutionarily conserved regulation of proteasome abundance.

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Authors and Affiliations

  1. Lynne Chantranupong and David M. Sabatini are at the Whitehead Institute, Cambridge, Massachusetts 02142, USA.,

    Lynne Chantranupong & David M. Sabatini

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  1. Lynne Chantranupong
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  2. David M. Sabatini
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Correspondence to Lynne Chantranupong or David M. Sabatini.

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Chantranupong, L., Sabatini, D. The TORC1 pathway to protein destruction. Nature 536, 155–156 (2016). https://doi.org/10.1038/nature18919

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