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Unraveling proteasome engagement

Authors :
Jonathan N. Pruneda
Cameron G. Roberts
Source :
Nature Chemical Biology. 16:813-815
Publication Year :
2020
Publisher :
Springer Science and Business Media LLC, 2020.

Abstract

A new study reveals that, in addition to its longstanding role in recruiting proteins to the proteasome, ubiquitination can also induce a structural destabilization that allows the target protein to be efficiently unraveled for degradation.

Subjects

Subjects :
0303 health sciences
biology
Chemistry
030302 biochemistry & molecular biology
food and beverages
Cell Biology
Cell biology
03 medical and health sciences
Proteasome
Ubiquitin
Mechanism of action
biology.protein
Posttranslational modification
medicine
Protein folding
Target protein
medicine.symptom
Molecular Biology
030304 developmental biology

Details

ISSN :
15524469 and 15524450
Volume :
16
Database :
OpenAIRE
Journal :
Nature Chemical Biology
Accession number :
edsair.doi...........58e04af64f07143e090006613357e55f
Full Text :
https://doi.org/10.1038/s41589-020-0573-2
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