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| Content Provider | PubMed Central |
|---|---|
| Author | Ripaud, Leslie Chumakova, Victoria Antonin, Matthias Hastie, Alex R. Pinkert, Stefan Körner, Roman Ruff, Kiersten M. Pappu, Rohit V. Hornburg, Daniel Mann, Matthias Hartl, F. Ulrich Hipp, Mark S. |
| Abstract | Expansion of a poly-glutamine (polyQ) repeat is the causal mutation of several inherited neurological disorders, including Huntington’s disease. In a yeast genetic screen, we identified several proteins with Q-rich, prion-like domains that reduce the toxicity of mutant polyQ proteins when overexpressed. One of these, glycine threonine serine repeat protein (Gts1p), was characterized in more detail. Association with Gts1p did not prevent aggregation but altered the physical properties and the interactome of the aggregates. Specifically, Gts1p expression reduced the sequestration of other prion-like proteins into the polyQ aggregates. These findings link polyQ toxicity in yeast with the coaggregation of prion proteins and show that short Q-rich peptides are able to shield toxic forms of polyQ proteins, directing them into nontoxic aggregates. |
| Related Links | http://dx.doi.org/10.1073/pnas.1421313111 |
| Ending Page | 18224 |
| Page Count | 6 |
| Starting Page | 18219 |
| File Format | |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 51 |
| Volume Number | 111 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2014-12-23 |
| Access Restriction | Open |
| Rights Holder | National Academy of Sciences |
| Subject Keyword | General Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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