Home > Articles > Published articles > Proteome response at the edge of protein aggregation |
Date: | 2015 |
Abstract: | 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. |
Grants: | European Commission 299105 Ministerio de Economía y Competitividad BFU2013-44763 Ministerio de Ciencia e Innovación AIB2010PT-00110 Ministerio de Ciencia e Innovación BFU2010-14901 |
Rights: | Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial, la distribució, la comunicació pública de l'obra i la creació d'obres derivades, fins i tot amb finalitats comercials, sempre i quan es reconegui l'autoria de l'obra original. |
Language: | Anglès |
Document: | Article ; recerca ; Versió publicada |
Subject: | Protein misfolding ; Oxidative stress ; Amyloid-β-peptide ; Proteomic response |
Published in: | Open biology, Vol. 5, issue 2 (Feb. 2015) , art. 140221, ISSN 2046-2441 |
9 p, 626.3 KB |