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  Stress- and ubiquitylation-dependent phase separation of the proteasome

Yasuda, S., Tsuchiya, H., Kaiho, A., Guo, Q., Ikeuchi, K., Endo, A., et al. (2020). Stress- and ubiquitylation-dependent phase separation of the proteasome. NATURE, 578, 296-300. doi:10.1038/s41586-020-1982-9.

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Yasuda, Sayaka1, Autor
Tsuchiya, Hikaru1, Autor
Kaiho, Ai1, Autor
Guo, Qiang2, Autor           
Ikeuchi, Ken1, Autor
Endo, Akinori1, Autor
Arai, Naoko1, Autor
Ohtake, Fumiaki1, Autor
Murata, Shigeo1, Autor
Inada, Toshifumi1, Autor
Baumeister, Wolfgang1, Autor
Fernandez-Busnadiego, Ruben2, Autor           
Tanaka, Keiji1, Autor
Saeki, Yasushi1, Autor
Affiliations:
1external, ou_persistent22              
2Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              

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Schlagwörter: 26S PROTEASOME; REVEALS; TOOLBOX; LOCALIZATION; DEGRADATION; SPECIFICITY; SOFTWARE; DYNAMICS
 Zusammenfassung: The proteasome is a major proteolytic machine that regulates cellular proteostasis through selective degradation of ubiquitylated proteins(1,2). A number of ubiquitin-related molecules have recently been found to be involved in the regulation of biomolecular condensates or membraneless organelles, which arise by liquid-liquid phase separation of specific biomolecules, including stress granules, nuclear speckles and autophagosomes(3-8), but it remains unclear whether the proteasome also participates in such regulation. Here we reveal that proteasome-containing nuclear foci form under acute hyperosmotic stress. These foci are transient structures that contain ubiquitylated proteins, p97 (also known as valosin-containing protein (VCP)) and multiple proteasome-interacting proteins, which collectively constitute a proteolytic centre. The major substrates for degradation by these foci were ribosomal proteins that failed to properly assemble. Notably, the proteasome foci exhibited properties of liquid droplets. RAD23B, a substrate-shuttling factor for the proteasome, and ubiquitylated proteins were necessary for formation of proteasome foci. In mechanistic terms, a liquid-liquid phase separation was triggered by multivalent interactions of two ubiquitin-associated domains of RAD23B and ubiquitin chains consisting of four or more ubiquitin molecules. Collectively, our results suggest that ubiquitin-chain-dependent phase separation induces the formation of a nuclear proteolytic compartment that promotes proteasomal degradation.
Hyperosmotic stress leads to a phase separation of the proteasome, triggered by interactions between RAD23B and ubiquitylated proteins, which bring together p97 and proteasome-associated proteins into nuclear proteolytic foci.

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Sprache(n): eng - English
 Datum: 2020-02
 Publikationsstatus: Online veröffentlicht
 Seiten: 5
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: ISI: 000511285700001
DOI: 10.1038/s41586-020-1982-9
 Art des Abschluß: -

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Titel: NATURE
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: MACMILLAN BUILDING, 4 CRINAN ST, LONDON N1 9XW, ENGLAND : NATURE PUBLISHING GROUP
Seiten: - Band / Heft: 578 Artikelnummer: - Start- / Endseite: 296 - 300 Identifikator: ISSN: 0028-0836