Legal but lethal: functional protein aggregation at the verge of toxicity

Many neurodegenerative disorders are linked to irreversible protein aggregation, a process that usually comes along with toxicity and serious cellular damage. However, it is emerging that protein aggregation can also serve for physiological purposes, as impressively shown for prions. While the aggre...

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Main Authors: S. Fabio eFalsone, Angelika eFalsone
Format: Article
Language:English
Published: Frontiers Media S.A. 2015-02-01
Series:Frontiers in Cellular Neuroscience
Subjects:
Online Access:http://journal.frontiersin.org/Journal/10.3389/fncel.2015.00045/full
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author S. Fabio eFalsone
Angelika eFalsone
author_facet S. Fabio eFalsone
Angelika eFalsone
author_sort S. Fabio eFalsone
collection DOAJ
description Many neurodegenerative disorders are linked to irreversible protein aggregation, a process that usually comes along with toxicity and serious cellular damage. However, it is emerging that protein aggregation can also serve for physiological purposes, as impressively shown for prions. While the aggregation of this protein family was initially considered exclusively toxic in mammalians organisms, it is now almost clear that many other proteins adopt prion-like attributes to rationally polymerise into higher order complexes with organised physiologic roles. This implies that cells can tolerate at least in some measure the accumulation of inherently dangerous protein aggregates for functional profit. This review summarises currently known strategies that living organisms adopt to preserve beneficial aggregation, and to prevent the catastrophic accumulation of toxic aggregates that frequently accompany neurodegeneration.
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spelling doaj.art-e9b33bf0f9d3428b8c7982c43af4aa192022-12-21T22:39:42ZengFrontiers Media S.A.Frontiers in Cellular Neuroscience1662-51022015-02-01910.3389/fncel.2015.00045118238Legal but lethal: functional protein aggregation at the verge of toxicityS. Fabio eFalsone0Angelika eFalsone1University of GrazUniversity of GrazMany neurodegenerative disorders are linked to irreversible protein aggregation, a process that usually comes along with toxicity and serious cellular damage. However, it is emerging that protein aggregation can also serve for physiological purposes, as impressively shown for prions. While the aggregation of this protein family was initially considered exclusively toxic in mammalians organisms, it is now almost clear that many other proteins adopt prion-like attributes to rationally polymerise into higher order complexes with organised physiologic roles. This implies that cells can tolerate at least in some measure the accumulation of inherently dangerous protein aggregates for functional profit. This review summarises currently known strategies that living organisms adopt to preserve beneficial aggregation, and to prevent the catastrophic accumulation of toxic aggregates that frequently accompany neurodegeneration.http://journal.frontiersin.org/Journal/10.3389/fncel.2015.00045/fullNeurodegenerative DiseasesPrionsAmyloidsproteostasis regulatorsproteotoxicity
spellingShingle S. Fabio eFalsone
Angelika eFalsone
Legal but lethal: functional protein aggregation at the verge of toxicity
Frontiers in Cellular Neuroscience
Neurodegenerative Diseases
Prions
Amyloids
proteostasis regulators
proteotoxicity
title Legal but lethal: functional protein aggregation at the verge of toxicity
title_full Legal but lethal: functional protein aggregation at the verge of toxicity
title_fullStr Legal but lethal: functional protein aggregation at the verge of toxicity
title_full_unstemmed Legal but lethal: functional protein aggregation at the verge of toxicity
title_short Legal but lethal: functional protein aggregation at the verge of toxicity
title_sort legal but lethal functional protein aggregation at the verge of toxicity
topic Neurodegenerative Diseases
Prions
Amyloids
proteostasis regulators
proteotoxicity
url http://journal.frontiersin.org/Journal/10.3389/fncel.2015.00045/full
work_keys_str_mv AT sfabioefalsone legalbutlethalfunctionalproteinaggregationatthevergeoftoxicity
AT angelikaefalsone legalbutlethalfunctionalproteinaggregationatthevergeoftoxicity