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New MAPS for misfolded proteins

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Clearing misfolded proteins from the cytoplasm is essential to maintain cellular homeostasis. Now, a parallel clearance system is described that uses the deubiquitylase USP19 to enable secretion of misfolded cytoplasmic proteins when conventional proteasomal degradation is compromised. Misfolding-associated protein secretion (MAPS) has important implications for protein quality control and prion-like transmission.

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Figure 1: Clearance of misfolded cytoplasmic proteins via the MAPS pathway.

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Authors and Affiliations

  1. Norbert Volkmar, Emma Fenech and John C. Christianson are at the Ludwig Institute for Cancer Research, University of Oxford, Oxford OX2 6TT, UK,

    Norbert Volkmar, Emma Fenech & John C. Christianson

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  1. Norbert Volkmar
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  2. Emma Fenech
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  3. John C. Christianson
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Contributions

N.V. and E.F. contributed equally to this work.

Corresponding author

Correspondence to John C. Christianson.

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The authors declare no competing financial interests.

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Volkmar, N., Fenech, E. & Christianson, J. New MAPS for misfolded proteins. Nat Cell Biol 18, 724–726 (2016). https://doi.org/10.1038/ncb3381

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