Unfolded protein stress in the endoplasmic reticulum and mitochondria: a role in neurodegeneration
Protein folding occurs in several intracellular locations including the endoplasmic reticulum (ER) and mitochondria. In normal conditions there is a balance between the levels of unfolded proteins and protein folding machinery. Disruption of homeostasis and an accumulation of unfolded proteins trigg...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2012-04-01
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| Series: | Frontiers in Aging Neuroscience |
| Subjects: | |
| Online Access: | http://journal.frontiersin.org/Journal/10.3389/fnagi.2012.00005/full |
| _version_ | 1818445607944060928 |
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| author | Sebastián eBernales Marisol Andrea Morales Soto Marisol Andrea Morales Soto Emma eMcCullagh |
| author_facet | Sebastián eBernales Marisol Andrea Morales Soto Marisol Andrea Morales Soto Emma eMcCullagh |
| author_sort | Sebastián eBernales |
| collection | DOAJ |
| description | Protein folding occurs in several intracellular locations including the endoplasmic reticulum (ER) and mitochondria. In normal conditions there is a balance between the levels of unfolded proteins and protein folding machinery. Disruption of homeostasis and an accumulation of unfolded proteins triggers stress responses, or unfolded protein responses (UPR), in these organelles. These pathways signal to increase the folding capacity, inhibit protein import or expression, increase protein degradation and potentially trigger cell death. Many aging-related neurodegenerative diseases involve the accumulation of misfolded proteins in both the ER and mitochondria. The exact participation of the UPRs in the onset of neurodegeneration is unclear, but there is significant evidence for the alteration of these pathways in the ER and mitochondria. Here we will discuss the involvement of ER and mitochondrial stress and the possible contributions of the UPR in these organelles to the development of two neurodegenerative diseases, Parkinson’s disease (PD) and Alzheimer’s disease (AD). |
| first_indexed | 2024-12-14T19:34:32Z |
| format | Article |
| id | doaj.art-aaed60c58ed240bb9f7af3a382103b8c |
| institution | Directory Open Access Journal |
| issn | 1663-4365 |
| language | English |
| last_indexed | 2024-12-14T19:34:32Z |
| publishDate | 2012-04-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Aging Neuroscience |
| spelling | doaj.art-aaed60c58ed240bb9f7af3a382103b8c2022-12-21T22:49:57ZengFrontiers Media S.A.Frontiers in Aging Neuroscience1663-43652012-04-01410.3389/fnagi.2012.0000525186Unfolded protein stress in the endoplasmic reticulum and mitochondria: a role in neurodegenerationSebastián eBernales0Marisol Andrea Morales Soto1Marisol Andrea Morales Soto2Emma eMcCullagh3Fundación Ciencia y VidaUniversidad Andrés BelloFundación Ciencia y VidaFundación Ciencia y VidaProtein folding occurs in several intracellular locations including the endoplasmic reticulum (ER) and mitochondria. In normal conditions there is a balance between the levels of unfolded proteins and protein folding machinery. Disruption of homeostasis and an accumulation of unfolded proteins triggers stress responses, or unfolded protein responses (UPR), in these organelles. These pathways signal to increase the folding capacity, inhibit protein import or expression, increase protein degradation and potentially trigger cell death. Many aging-related neurodegenerative diseases involve the accumulation of misfolded proteins in both the ER and mitochondria. The exact participation of the UPRs in the onset of neurodegeneration is unclear, but there is significant evidence for the alteration of these pathways in the ER and mitochondria. Here we will discuss the involvement of ER and mitochondrial stress and the possible contributions of the UPR in these organelles to the development of two neurodegenerative diseases, Parkinson’s disease (PD) and Alzheimer’s disease (AD).http://journal.frontiersin.org/Journal/10.3389/fnagi.2012.00005/fullEndoplasmic ReticulumMitochondriaUnfolded Protein ResponseParkinson’s diseaseneurodegenerationAlzheimer’s disease |
| spellingShingle | Sebastián eBernales Marisol Andrea Morales Soto Marisol Andrea Morales Soto Emma eMcCullagh Unfolded protein stress in the endoplasmic reticulum and mitochondria: a role in neurodegeneration Frontiers in Aging Neuroscience Endoplasmic Reticulum Mitochondria Unfolded Protein Response Parkinson’s disease neurodegeneration Alzheimer’s disease |
| title | Unfolded protein stress in the endoplasmic reticulum and mitochondria: a role in neurodegeneration |
| title_full | Unfolded protein stress in the endoplasmic reticulum and mitochondria: a role in neurodegeneration |
| title_fullStr | Unfolded protein stress in the endoplasmic reticulum and mitochondria: a role in neurodegeneration |
| title_full_unstemmed | Unfolded protein stress in the endoplasmic reticulum and mitochondria: a role in neurodegeneration |
| title_short | Unfolded protein stress in the endoplasmic reticulum and mitochondria: a role in neurodegeneration |
| title_sort | unfolded protein stress in the endoplasmic reticulum and mitochondria a role in neurodegeneration |
| topic | Endoplasmic Reticulum Mitochondria Unfolded Protein Response Parkinson’s disease neurodegeneration Alzheimer’s disease |
| url | http://journal.frontiersin.org/Journal/10.3389/fnagi.2012.00005/full |
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