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Home Search Quick Search Advanced Fulltext Browse Collections Persons My eDoc Session History Login Name: Password: Documentation Help Support Wiki Direct access to document ID:	Institute: MPI für molekulare Zellbiologie und Genetik     Collection: MPI-CBG Publications 2015 (arch)     Display Documents ID: 717999.0, MPI für molekulare Zellbiologie und Genetik / MPI-CBG Publications 2015 (arch) A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation. Authors: Patel, Avinash; Lee, Hyun-Ok Kate; Jawerth, Louise; Maharana, Shovamayee; Jahnel, Marcus; Hein, Marco Y; Stoynov, Stoyno; Mahamid, J.; Saha, Shambaditya; Franzmann, Titus; Pozniakovski, Andrei; Poser, Ina; Maghelli, Nicola; Royer, Loic; Weigert, Martin; Myers, Eugene W; Grill, Stephan W.; Drechsel, David N.; Hyman, Anthony; Alberti, Simon Date of Publication (YYYY-MM-DD): 2015 Title of Journal: Cell Volume: 162 Issue / Number: 5 Start Page: 1066 End Page: 1077 Copyright: not available Audience: Experts Only Intended Educational Use: No Abstract / Description: Many proteins contain disordered regions of low-sequence complexity, which cause aging-associated diseases because they are prone to aggregate. Here, we study FUS, a prion-like protein containing intrinsically disordered domains associated with the neurodegenerative disease ALS. We show that, in cells, FUS forms liquid compartments at sites of DNA damage and in the cytoplasm upon stress. We confirm this by reconstituting liquid FUS compartments in vitro. Using an in vitro "aging" experiment, we demonstrate that liquid droplets of FUS protein convert with time from a liquid to an aggregated state, and this conversion is accelerated by patient-derived mutations. We conclude that the physiological role of FUS requires forming dynamic liquid-like compartments. We propose that liquid-like compartments carry the trade-off between functionality and risk of aggregation and that aberrant phase transitions within liquid-like compartments lie at the heart of ALS and, presumably, other age-related diseases. VIDEO ABSTRACT. External Publication Status: published Document Type: Article Communicated by: Thüm Affiliations: MPI für molekulare Zellbiologie und Genetik Identifiers: LOCALID:6272 The scope and number of records on eDoc is subject to the collection policies defined by each institute - see "info" button in the collection browse view.