Deubiquitinase activity is required for the proteasomal degradation of misfolded cytosolic proteins upon heat-stress
Ubiquitination of misfolded proteins usually results in protein degradation. Here, the authors show that two deubiquitinases—enzymes that remove ubiquitin—are required for the proteasomal degradation of misfolded proteins in response to heat-shock in yeast.
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Publishing Group
2016-10-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/ncomms12907 |
| Summary: | Ubiquitination of misfolded proteins usually results in protein degradation. Here, the authors show that two deubiquitinases—enzymes that remove ubiquitin—are required for the proteasomal degradation of misfolded proteins in response to heat-shock in yeast. |
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| ISSN: | 2041-1723 |