Proteome response at the edge of protein aggregation
Proteins adopt defined structures and are crucial to most cellular functions. Their misfolding and aggregation is associated with numerous degenerative human disorders such as type II diabetes, Huntington's or Alzheimer's diseases. Here, we aim to understand why cells promote the formation...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
The Royal Society
2015-01-01
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| Series: | Open Biology |
| Subjects: | |
| Online Access: | https://royalsocietypublishing.org/doi/pdf/10.1098/rsob.140221 |
| _version_ | 1818966983572455424 |
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| author | Natalia Sanchez de Groot Ricardo A. Gomes Anna Villar-Pique M. Madan Babu Ana Varela Coelho Salvador Ventura |
| author_facet | Natalia Sanchez de Groot Ricardo A. Gomes Anna Villar-Pique M. Madan Babu Ana Varela Coelho Salvador Ventura |
| author_sort | Natalia Sanchez de Groot |
| collection | DOAJ |
| description | Proteins adopt defined structures and are crucial to most cellular functions. Their misfolding and aggregation is associated with numerous degenerative human disorders such as type II diabetes, Huntington's or Alzheimer's diseases. Here, we aim to understand why cells promote the formation of protein foci. Comparison of two amyloid-β-peptide variants, mostly insoluble but differently recruited by the cell (inclusion body versus diffused), reveals small differences in cell fitness and proteome response. We suggest that the levels of oxidative stress act as a sensor to trigger protein recruitment into foci. Our data support a common cytoplasmic response being able to discern and react to the specific properties of polypeptides. |
| first_indexed | 2024-12-20T13:41:34Z |
| format | Article |
| id | doaj.art-8ebcc5705e254bab9252f13dde34a7aa |
| institution | Directory Open Access Journal |
| issn | 2046-2441 |
| language | English |
| last_indexed | 2024-12-20T13:41:34Z |
| publishDate | 2015-01-01 |
| publisher | The Royal Society |
| record_format | Article |
| series | Open Biology |
| spelling | doaj.art-8ebcc5705e254bab9252f13dde34a7aa2022-12-21T19:38:47ZengThe Royal SocietyOpen Biology2046-24412015-01-015210.1098/rsob.140221140221Proteome response at the edge of protein aggregationNatalia Sanchez de GrootRicardo A. GomesAnna Villar-PiqueM. Madan BabuAna Varela CoelhoSalvador VenturaProteins adopt defined structures and are crucial to most cellular functions. Their misfolding and aggregation is associated with numerous degenerative human disorders such as type II diabetes, Huntington's or Alzheimer's diseases. Here, we aim to understand why cells promote the formation of protein foci. Comparison of two amyloid-β-peptide variants, mostly insoluble but differently recruited by the cell (inclusion body versus diffused), reveals small differences in cell fitness and proteome response. We suggest that the levels of oxidative stress act as a sensor to trigger protein recruitment into foci. Our data support a common cytoplasmic response being able to discern and react to the specific properties of polypeptides.https://royalsocietypublishing.org/doi/pdf/10.1098/rsob.140221protein misfoldingoxidative stressamyloid-β-peptideproteomic response |
| spellingShingle | Natalia Sanchez de Groot Ricardo A. Gomes Anna Villar-Pique M. Madan Babu Ana Varela Coelho Salvador Ventura Proteome response at the edge of protein aggregation Open Biology protein misfolding oxidative stress amyloid-β-peptide proteomic response |
| title | Proteome response at the edge of protein aggregation |
| title_full | Proteome response at the edge of protein aggregation |
| title_fullStr | Proteome response at the edge of protein aggregation |
| title_full_unstemmed | Proteome response at the edge of protein aggregation |
| title_short | Proteome response at the edge of protein aggregation |
| title_sort | proteome response at the edge of protein aggregation |
| topic | protein misfolding oxidative stress amyloid-β-peptide proteomic response |
| url | https://royalsocietypublishing.org/doi/pdf/10.1098/rsob.140221 |
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