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- Eisele, FrederikGothenburg University,Göteborgs universitet,Institutionen för biomedicin,Institute of Biomedicine (author)
An Hsp90 co-chaperone links protein folding and degradation and is part of a conserved protein quality control
- Article/chapterEnglish2021
Publisher, publication year, extent ...
- Elsevier BV,2021
Numbers
- LIBRIS-ID:oai:gup.ub.gu.se/306482
- https://gup.ub.gu.se/publication/306482URI
- https://doi.org/10.1016/j.celrep.2021.109328DOI
- https://res.slu.se/id/publ/114684URI
Supplementary language notes
- Language:English
Part of subdatabase
- SwePubSwePub
Classification
Notes
- In this paper, we show that the essential Hsp90 co-chaperone Sgt1 is a member of a general protein quality control network that links folding and degradation through its participation in the degradation of misfolded proteins both in the cytosol and the endoplasmic reticulum (ER). Sgt1-dependent protein degradation acts in a parallel pathway to the ubiquitin ligase (E3) and ubiquitin chain elongase (E4), Hul5, and overproduction of Hul5 partly suppresses defects in cells with reduced Sgt1 activity. Upon proteostatic stress, Sgt1 accumulates transiently, in an Hsp90- and proteasome-dependent manner, with quality control sites (Q-bodies) of both yeast and human cells that co-localize with Vps13, a protein that creates organelle contact sites. Misfolding disease proteins, such as synphilin-1 involved in Parkinson's disease, are also sequestered to these compartments and require Sgt1 for their clearance. © 2021 The Author(s)
Subject headings and genre
- MEDICIN OCH HÄLSOVETENSKAP Klinisk medicin hsv//swe
- MEDICAL AND HEALTH SCIENCES Clinical Medicine hsv//eng
- NATURVETENSKAP Biologi Cellbiologi hsv//swe
- NATURAL SCIENCES Biological Sciences Cell Biology hsv//eng
- 26S proteasome
- aging
- chaperone
- Hsp90
- Hul5
- protein quality control
- proteostasis
- Sgt1
- heat shock protein 90
- Hul5 protein
- peptides and proteins
- proteasome
- protein serine threonine kinase
- Sgt1 protein
- synphilin 1
- ubiquitin protein ligase
- ubiquitin protein ligase E3
- unclassified drug
- Vps13 protein
- Article
- cell growth
- controlled study
- cytosol
- endoplasmic reticulum
- enzyme activity
- HeLa cell line
- human
- human cell
- nonhuman
- Parkinson disease
- protein aggregation
- protein degradation
- protein expression
- protein folding
- protein homeostasis
- protein localization
- protein quality
- yeast cell
Added entries (persons, corporate bodies, meetings, titles ...)
- Eisele-Bürger, Anna MariaSwedish University of Agricultural Sciences,Sveriges lantbruksuniversitet,Gothenburg University,Göteborgs universitet,Institutionen för biomedicin,Institute of Biomedicine,Institutionen för Molekylära vetenskaper,Department of Molecular Sciences,University of Gothenburg(Swepub:gu)xeisea (author)
- Hao, XinxinGothenburg University,Göteborgs universitet,Institutionen för biomedicin,Institute of Biomedicine(Swepub:gu)xxinha (author)
- Larsson Berglund, LisaGothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology(Swepub:gu)xllism (author)
- Höög, Johanna L,1979Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology(Swepub:gu)xhoojo (author)
- Liu, Beidong,1972Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology(Swepub:gu)xbeili (author)
- Nyström, Thomas,1960Gothenburg University,Göteborgs universitet,Institutionen för biomedicin,Institute of Biomedicine(Swepub:gu)xnysth (author)
- Göteborgs universitetInstitutionen för biomedicin (creator_code:org_t)
- Sveriges lantbruksuniversitet
Related titles
- In:Cell Reports: Elsevier BV35:132211-1247
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