FUS Zigzags Its Way to Cross Beta

Alex S Holehouse; Rohit V Pappu

doi:10.1016/j.cell.2017.10.007

FUS Zigzags Its Way to Cross Beta

Cell. 2017 Oct 19;171(3):499-500. doi: 10.1016/j.cell.2017.10.007.

Authors

Alex S Holehouse¹, Rohit V Pappu²

Affiliations

¹ Department of Biomedical Engineering and Center for Biological Systems Engineering, Washington University in Saint Louis, Saint Louis, MO 63130, USA.
² Department of Biomedical Engineering and Center for Biological Systems Engineering, Washington University in Saint Louis, Saint Louis, MO 63130, USA. Electronic address: [email protected].

PMID: 29053965
DOI: 10.1016/j.cell.2017.10.007

Abstract

The low-complexity domain (LCD) of the FUS protein forms concentration-dependent assemblies, including liquid droplets and fibril-based hydrogels. The molecular structures of FUS within different assemblies and their functional relevance are subjects of intense debate. Murray et al. report an atomic-level structural model for FUS LCD fibrils that answers some questions and raises new ones.

Publication types

Comment

MeSH terms

RNA-Binding Protein FUS*

Substances

RNA-Binding Protein FUS