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Molecular genetics

Chaperone protein gets personal

Nature volume 545, pages 36–37 (2017)Cite this article

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Two studies of the molecular chaperone protein HSP90 reveal how complex traits can be shaped by genetic and environmental context. This work highlights the challenges of personalized medicine.

The effects of a disease-causing genetic mutation may differ between individuals because of differences at other genes or in the environments those individuals have experienced. For example, hundreds of mutations can cause Fanconi anaemia, a blood-cell deficiency that predisposes people to cancer, but the mutation a patient harbours is a very poor predictor of whether they will have mild or severe disease1. Understanding how context alters outcomes in this way lies at the heart of personalized medicine2. Two studies (one in Cell3 and one in Nature Structural and Molecular Biology4) now provide compelling mechanisms by which heat-shock protein 90 (HSP90) alters outcomes associated with genetic differences.

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Figure 1: Heat-shock protein 90 (HSP90) alters the effects of genetic differences.

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Authors and Affiliations

  1. Department of Biology, Center for Genomics and Systems Biology, New York University, New York, 10003, New York, USA

    Mark L. Siegal

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  1. Mark L. Siegal
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Correspondence to Mark L. Siegal.

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Siegal, M. Chaperone protein gets personal. Nature 545, 36–37 (2017). https://doi.org/10.1038/nature22487

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