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Preserving protein function through reversible aggregation

Nature Cell Biology volume 19, pages 1142–1144 (2017)Cite this article

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It is generally accepted that protein function depends on a defined 3D structure, with unfolding and aggregation dealing a final blow to functionality. A study now shows that the regulated exposure of an unstructured region in yeast pyruvate kinase triggers reversible aggregation to preserve protein function under stress.

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Figure 1: Glucose starvation causes a reversible phase transition of the yeast pyruvate kinase Cdc19 from a soluble to a solid amyloid-like state.

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  1. Institute for Cell Biology, University of Bonn, Ulrich-Haberland-Str. 61a, Bonn, D-53121, Germany

    Jörg Höhfeld

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  1. Jörg Höhfeld
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Correspondence to Jörg Höhfeld.

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The author declares no competing financial interests.

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Höhfeld, J. Preserving protein function through reversible aggregation. Nat Cell Biol 19, 1142–1144 (2017). https://doi.org/10.1038/ncb3620

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