Molecular mechanisms of spatial protein quality control
Research output: Contribution to journal › Review article › Contributed › peer-review
Contributors
Abstract
Evidence is now accumulating that damaged proteins are not randomly distributed but often concentrated in microscopically visible and functionally distinct inclusion bodies. How misfolded proteins are organized into these compartments, however, is still unknown. We have recently begun to investigate stress-inducible protein quality control (PQC) bodies in yeast cells. Surprisingly, we found that protein misfolding and aggregation were not sufficient to trigger body formation under mild heat stress conditions. Rather, compartment assembly also required the concerted action of molecular chaperones, protein-sorting factors and protein-sequestration factors, thus defining a minimal machinery for spatial PQC. Expression of this machinery was limited to times of acute stress through rapid changes in mRNA abundance and a proteasomal feedback mechanism. These findings demonstrate that yeast cells can control the amount of soluble misfolded proteins through regulated phase transitions in the cytoplasm, thus allowing them to rapidly adapt to changing environmental conditions.
Details
Original language | English |
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Pages (from-to) | 437-442 |
Number of pages | 6 |
Journal | PRION |
Volume | 6 |
Issue number | 5 |
Publication status | Published - Nov 2012 |
Peer-reviewed | Yes |
Externally published | Yes |
External IDs
PubMed | 23051707 |
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ORCID | /0000-0003-4017-6505/work/161409865 |
Keywords
Sustainable Development Goals
ASJC Scopus subject areas
Keywords
- Amyloid, Btn2, Cur1, Hsp104, Hsp40, Hsp42, IPOD, JUNQ, Molecular chaperone, Prion, Proteasome, Protein aggregation, Protein quality control, Sis1, Ubiquitin