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Sending protein aggregates into a downward spiral

Nature Structural & Molecular Biology volume 23, pages 769–770 (2016)Cite this article

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Cells deploy the Hsp100 family of ATP-dependent machines to work with cellular chaperones in dismantling dangerous protein aggregates. New studies reveal an unprecedented spiral structure that provides mechanistic insight into the protein disaggregase Hsp104.

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Figure 1: AAA+ enzymes can form diverse double-ring spirals.
Figure 2: Examples of helical architectures across diverse AAA+ enzymes.

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Acknowledgements

The authors thank J. Rubenstein for sharing coordinates before release. Work in the authors' laboratories is supported by NIH grants R01GM111706 (P.C.) and R01GM115898 (S.E.G.).

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Authors and Affiliations

  1. Steven E. Glynn is at the Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, New York, USA.,

    Steven E Glynn

  2. Peter Chien is at the Department of Biochemistry and Molecular Biology, University of Massachusetts Amherst, Amherst, Massachusetts, USA.,

    Peter Chien

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  1. Steven E Glynn
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  2. Peter Chien
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Correspondence to Steven E Glynn or Peter Chien.

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Glynn, S., Chien, P. Sending protein aggregates into a downward spiral. Nat Struct Mol Biol 23, 769–770 (2016). https://doi.org/10.1038/nsmb.3288

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