Understanding and exploiting interactions between cellular proteostasis pathways and infectious prion proteins for therapeutic benefit
Several neurodegenerative diseases of humans and animals are caused by the misfolded prion protein (PrP ), a self-propagating protein infectious agent that aggregates into oligomeric, fibrillar structures and leads to cell death by incompletely understood mechanisms. Work in multiple biological mode...
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Published in | Open biology Vol. 10; no. 11; p. 200282 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
England
The Royal Society
01.11.2020
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Subjects | |
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Abstract | Several neurodegenerative diseases of humans and animals are caused by the misfolded prion protein (PrP
), a self-propagating protein infectious agent that aggregates into oligomeric, fibrillar structures and leads to cell death by incompletely understood mechanisms. Work in multiple biological model systems, from simple baker's yeast to transgenic mouse lines, as well as
studies, has illuminated molecular and cellular modifiers of prion disease. In this review, we focus on intersections between PrP and the proteostasis network, including unfolded protein stress response pathways and roles played by the powerful regulators of protein folding known as protein chaperones. We close with analysis of promising therapeutic avenues for treatment enabled by these studies. |
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AbstractList | Several neurodegenerative diseases of humans and animals are caused by the misfolded prion protein (PrP
Sc
), a self-propagating protein infectious agent that aggregates into oligomeric, fibrillar structures and leads to cell death by incompletely understood mechanisms. Work in multiple biological model systems, from simple baker's yeast to transgenic mouse lines, as well as
in vitro
studies, has illuminated molecular and cellular modifiers of prion disease. In this review, we focus on intersections between PrP and the proteostasis network, including unfolded protein stress response pathways and roles played by the powerful regulators of protein folding known as protein chaperones. We close with analysis of promising therapeutic avenues for treatment enabled by these studies. Several neurodegenerative diseases of humans and animals are caused by the misfolded prion protein (PrP ), a self-propagating protein infectious agent that aggregates into oligomeric, fibrillar structures and leads to cell death by incompletely understood mechanisms. Work in multiple biological model systems, from simple baker's yeast to transgenic mouse lines, as well as studies, has illuminated molecular and cellular modifiers of prion disease. In this review, we focus on intersections between PrP and the proteostasis network, including unfolded protein stress response pathways and roles played by the powerful regulators of protein folding known as protein chaperones. We close with analysis of promising therapeutic avenues for treatment enabled by these studies. Several neurodegenerative diseases of humans and animals are caused by the misfolded prion protein (PrPSc), a self-propagating protein infectious agent that aggregates into oligomeric, fibrillar structures and leads to cell death by incompletely understood mechanisms. Work in multiple biological model systems, from simple baker's yeast to transgenic mouse lines, as well as in vitro studies, has illuminated molecular and cellular modifiers of prion disease. In this review, we focus on intersections between PrP and the proteostasis network, including unfolded protein stress response pathways and roles played by the powerful regulators of protein folding known as protein chaperones. We close with analysis of promising therapeutic avenues for treatment enabled by these studies. |
Author | Morano, Kevin A Catumbela, Celso S G Yakubu, Unekwu M Morales, Rodrigo |
AuthorAffiliation | 3 Mitchell Center for Alzheimer's Disease and Related Brain Disorders, Department of Neurology, McGovern Medical School at UTHealth , Houston, TX USA 2 MD Anderson UTHealth Graduate School at UTHealth , Houston, TX USA 4 Centro integrativo de biología y química aplicada (CIBQA), Universidad Bernardo O'Higgins , Santiago , Chile 1 Department of Microbiology and Molecular Genetics, McGovern Medical School at UTHealth , Houston, TX USA |
AuthorAffiliation_xml | – name: 1 Department of Microbiology and Molecular Genetics, McGovern Medical School at UTHealth , Houston, TX USA – name: 2 MD Anderson UTHealth Graduate School at UTHealth , Houston, TX USA – name: 3 Mitchell Center for Alzheimer's Disease and Related Brain Disorders, Department of Neurology, McGovern Medical School at UTHealth , Houston, TX USA – name: 4 Centro integrativo de biología y química aplicada (CIBQA), Universidad Bernardo O'Higgins , Santiago , Chile |
Author_xml | – sequence: 1 givenname: Unekwu M surname: Yakubu fullname: Yakubu, Unekwu M organization: MD Anderson UTHealth Graduate School at UTHealth, Houston, TX USA – sequence: 2 givenname: Celso S G surname: Catumbela fullname: Catumbela, Celso S G organization: Mitchell Center for Alzheimer's Disease and Related Brain Disorders, Department of Neurology, McGovern Medical School at UTHealth, Houston, TX USA – sequence: 3 givenname: Rodrigo surname: Morales fullname: Morales, Rodrigo organization: Centro integrativo de biología y química aplicada (CIBQA), Universidad Bernardo O'Higgins, Santiago, Chile – sequence: 4 givenname: Kevin A surname: Morano fullname: Morano, Kevin A organization: Department of Microbiology and Molecular Genetics, McGovern Medical School at UTHealth, Houston, TX USA |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/33234071$$D View this record in MEDLINE/PubMed |
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CitedBy_id | crossref_primary_10_1016_j_jbc_2021_100567 |
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Keywords | stress prions protein chaperones human protein misfolding yeast |
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Snippet | Several neurodegenerative diseases of humans and animals are caused by the misfolded prion protein (PrP
), a self-propagating protein infectious agent that... Several neurodegenerative diseases of humans and animals are caused by the misfolded prion protein (PrP Sc ), a self-propagating protein infectious agent that... Several neurodegenerative diseases of humans and animals are caused by the misfolded prion protein (PrPSc), a self-propagating protein infectious agent that... |
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SubjectTerms | human prions protein chaperones protein misfolding Review stress yeast |
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Title | Understanding and exploiting interactions between cellular proteostasis pathways and infectious prion proteins for therapeutic benefit |
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