Intramolecular Interactions between Folded and Disordered Regions Shape Ubiquilin Structure and Function
Jessica K Niblo, Nirbhik Acharya, Maxwell B Watkins, Carlos A Castañeda, Shahar Sukenik · 2026
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Description
Jessica K Niblo and colleagues studied in 2026 how floppy protein segments interact with folded parts in multi domain proteins. These flexible regions, joined to structured domains, give proteins unusual shapes and jobs, but their effect on overall structure has stayed unclear. The team focused on ubiquilins, proteins that carry damaged cargo to the cell recycling machinery.
Using biophysical tests and computer models, starting with the yeast version called Dsk2, they measured contacts between disordered tails and folded domains. The contacts shape how ubiquilins fold, move, and bind cargo. The findings help explain protein quality control and why its failure can harm cells, with lessons for diseases tied to faulty protein disposal.
Catalog record
| CREATOR | Jessica K Niblo, Nirbhik Acharya, Maxwell B Watkins, Carlos A Castañeda, Shahar Sukenik |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 65 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |