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| Verfasst von: | Grousl, Tomas [VerfasserIn]  |
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| | Ungelenk, Sophia Maria [VerfasserIn] |
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| | Ho, Chi-Ting [VerfasserIn] |
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| | Khokhrina, Maria [VerfasserIn] |
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| | Mayer, Matthias P. [VerfasserIn] |
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| | Bukau, Bernd [VerfasserIn] |
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| | Mogk, Axel [VerfasserIn] |
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| Titel: | A prion-like domain in Hsp42 drives chaperone-facilitated aggregation of misfolded proteins |
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| Verf.angabe: | Tomas Grousl, Sophia Ungelenk, Stephanie Miller, Chi-Ting Ho, Maria Khokhrina, Matthias P. Mayer, Bernd Bukau, and Axel Mogk |
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| E-Jahr: | 2018 |
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| Jahr: | January 23, 2018 |
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| Umfang: | 17 S. |
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| Fussnoten: | Gesehen am 20.05.2019 |
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| Titel Quelle: | Enthalten in: The journal of cell biology |
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| Ort Quelle: | New York, NY : Rockefeller Univ. Press, 1962 |
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| Jahr Quelle: | 2018 |
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| Band/Heft Quelle: | 217(2018), 4, Seite 1269-1285 |
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| ISSN Quelle: | 1540-8140 |
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| Abstract: | Chaperones with aggregase activity promote and organize the aggregation of misfolded proteins and their deposition at specific intracellular sites. This activity represents a novel cytoprotective strategy of protein quality control systems; however, little is known about its mechanism. In yeast, the small heat shock protein Hsp42 orchestrates the stress-induced sequestration of misfolded proteins into cytosolic aggregates (CytoQ). In this study, we show that Hsp42 harbors a prion-like domain (PrLD) and a canonical intrinsically disordered domain (IDD) that act coordinately to promote and control protein aggregation. Hsp42 PrLD is essential for CytoQ formation and is bifunctional, mediating self-association as well as binding to misfolded proteins. Hsp42 IDD confines chaperone and aggregase activity and affects CytoQ numbers and stability in vivo. Hsp42 PrLD and IDD are both crucial for cellular fitness during heat stress, demonstrating the need for sequestering misfolded proteins in a regulated manner. |
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| DOI: | doi:10.1083/jcb.201708116 |
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| URL: | Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.
Volltext ; Verlag: https://doi.org/10.1083/jcb.201708116 |
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| | Volltext: http://jcb.rupress.org/content/217/4/1269 |
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| | DOI: https://doi.org/10.1083/jcb.201708116 |
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| Datenträger: | Online-Ressource |
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| Sprache: | eng |
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| K10plus-PPN: | 1665935529 |
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| Verknüpfungen: | → Zeitschrift |
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¬A¬ prion-like domain in Hsp42 drives chaperone-facilitated aggregation of misfolded proteins / Grousl, Tomas [VerfasserIn]; January 23, 2018 (Online-Ressource)
