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 (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 mod...
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The Royal Society
2020-11-01
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doaj-c199c6653517451893515d2f0fc3b1b82021-01-15T14:15:12ZengThe Royal SocietyOpen Biology2046-24412020-11-01101110.1098/rsob.200282200282Understanding and exploiting interactions between cellular proteostasis pathways and infectious prion proteins for therapeutic benefitUnekwu M. YakubuCelso S. G. CatumbelaRodrigo MoralesKevin A. MoranoSeveral 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.https://royalsocietypublishing.org/doi/pdf/10.1098/rsob.200282prionsprotein chaperoneshumanyeaststressprotein misfolding |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Unekwu M. Yakubu Celso S. G. Catumbela Rodrigo Morales Kevin A. Morano |
spellingShingle |
Unekwu M. Yakubu Celso S. G. Catumbela Rodrigo Morales Kevin A. Morano Understanding and exploiting interactions between cellular proteostasis pathways and infectious prion proteins for therapeutic benefit Open Biology prions protein chaperones human yeast stress protein misfolding |
author_facet |
Unekwu M. Yakubu Celso S. G. Catumbela Rodrigo Morales Kevin A. Morano |
author_sort |
Unekwu M. Yakubu |
title |
Understanding and exploiting interactions between cellular proteostasis pathways and infectious prion proteins for therapeutic benefit |
title_short |
Understanding and exploiting interactions between cellular proteostasis pathways and infectious prion proteins for therapeutic benefit |
title_full |
Understanding and exploiting interactions between cellular proteostasis pathways and infectious prion proteins for therapeutic benefit |
title_fullStr |
Understanding and exploiting interactions between cellular proteostasis pathways and infectious prion proteins for therapeutic benefit |
title_full_unstemmed |
Understanding and exploiting interactions between cellular proteostasis pathways and infectious prion proteins for therapeutic benefit |
title_sort |
understanding and exploiting interactions between cellular proteostasis pathways and infectious prion proteins for therapeutic benefit |
publisher |
The Royal Society |
series |
Open Biology |
issn |
2046-2441 |
publishDate |
2020-11-01 |
description |
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. |
topic |
prions protein chaperones human yeast stress protein misfolding |
url |
https://royalsocietypublishing.org/doi/pdf/10.1098/rsob.200282 |
work_keys_str_mv |
AT unekwumyakubu understandingandexploitinginteractionsbetweencellularproteostasispathwaysandinfectiousprionproteinsfortherapeuticbenefit AT celsosgcatumbela understandingandexploitinginteractionsbetweencellularproteostasispathwaysandinfectiousprionproteinsfortherapeuticbenefit AT rodrigomorales understandingandexploitinginteractionsbetweencellularproteostasispathwaysandinfectiousprionproteinsfortherapeuticbenefit AT kevinamorano understandingandexploitinginteractionsbetweencellularproteostasispathwaysandinfectiousprionproteinsfortherapeuticbenefit |
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1724336873406464000 |