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One domain fits all: Using disordered regions to sequester misfolded proteins.

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Boczek,  Edgar
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

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Alberti,  Simon
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

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Citation

Boczek, E., & Alberti, S. (2018). One domain fits all: Using disordered regions to sequester misfolded proteins. The Journal of cell biology, 217(4), 1173-1175. doi:10.1083/jcb.201803015.


Cite as: https://hdl.handle.net/21.11116/0000-0003-F5AD-6
Abstract
Small heat shock proteins (sHsps) are adenosine triphosphate-independent chaperones that protect cells from misfolded proteins. In this issue, Grousl et al. (2018.J. Cell Biol.https://doi.org/10.1083/jcb.201708116) show that the yeast sHsp Hsp42 uses a prion-like intrinsically disordered domain to bind and sequester misfolded proteins in protein deposition sites.