期刊
MOLECULAR CELL
卷 71, 期 2, 页码 216-+出版社
CELL PRESS
DOI: 10.1016/j.molcel.2018.07.008
关键词
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资金
- National Institutes of Health [R35 GM119544]
- National Ataxia Foundation
- NIH [F31 NS098754, R01 GM067180]
- Research and Education Program, a component of the Advancing a Healthier Wisconsin endowment at the Medical College of Wisconsin
- Sophia Wolfe Quadracci Memorial Fellowship
The polyglutamine (polyQ) diseases are a group of nine neurodegenerative diseases caused by the expansion of a polyQ tract that results in protein aggregation. Unlike other model organisms, Dictyostelium discoideum is a proteostatic outlier, naturally encoding long polyQ tracts yet resistant to polyQ aggregation. Here we identify serine-rich chaperone protein 1 (SRCP1) as a molecular chaperone that is necessary and sufficient to suppress polyQ aggregation. SRCP1 inhibits aggregation of polyQ-expanded proteins, allowing for their degradation via the proteasome, where SRCP1 is also degraded. SRCP1's C-terminal domain is essential for its activity in cells, and peptides that mimic this domain suppress polyQ aggregation in vitro. Together our results identify a novel type of molecular chaperone and reveal how nature has dealt with the problem of polyQ aggregation.
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