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Structural biology

Signalling from disordered proteins

Nature volume 498, pages 308–310 (2013)Cite this article

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The discovery that a disordered protein can transmit signals between two binding sites calls into question the idea that communication within proteins requires a specific structural pathway linking such sites. See Letter p.390

Signalling is at the heart of biology, and most of it is mediated by proteins. However, despite recent progress in identifying the component proteins of many signalling networks1, and in our understanding of the complexities of such networks, how individual proteins fulfil their role in a particular network is still not well understood. On page 390 of this issue, Ferreon et al.2 show that intrinsically disordered proteins — which lack well-defined tertiary structures3, unlike their structured protein counterparts — can not only regulate the magnitude of a particular signal, but also reverse it, transforming a positive effector into a negative one. This result reinforces an emerging view that such proteins play a crucial part in signalling4, and challenges much of the current dogma about the relationship between protein structure and function, and the role that specific structural pathways have in signalling.

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Figure 1: The structural view of allostery.
Figure 2: The ensemble view of allostery.

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  1. Vincent J. Hilser is in the Departments of Biology and Biophysics, Johns Hopkins University, Baltimore, Maryland 21218, USA.,

    Vincent J. Hilser

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  1. Vincent J. Hilser
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Correspondence to Vincent J. Hilser.

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Hilser, V. Signalling from disordered proteins. Nature 498, 308–310 (2013). https://doi.org/10.1038/498308a

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