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dc.contributor.authorSaarikangas, Jen_US
dc.contributor.authorCaudron, Fen_US
dc.date.accessioned2018-01-19T10:51:40Z
dc.date.available2017-04-18en_US
dc.date.issued2017-05-04en_US
dc.date.submitted2017-12-19T13:32:33.640Z
dc.identifier.urihttp://qmro.qmul.ac.uk/xmlui/handle/123456789/31429
dc.description.abstractOrganisms rely on correctly folded proteins to carry out essential functions. Protein quality control factors guard proteostasis and prevent protein misfolding. When quality control fails and in response to diverse stresses, many proteins start to accumulate at specific deposit sites that maintain cellular organization and protect the functionality of coalescing proteins. These transitions involve dedicated proteins that promote coalescence and are facilitated by endo-membranes and cytoskeletal platforms. Moreover, several proteins make use of weak multivalent interactions or conformational templating to drive the formation of large-scale assemblies. Formation of such assemblies is often associated with a change in biochemical activity that can be used by cells to execute biochemical decisions in a localized manner during development and adaption. Since all assembly types impact cell physiology, their localization and dynamics need to be tightly regulated. Interestingly, at least some of the regulatory mechanisms are shared by functional membrane-less organelles and assemblies of terminally aggregated proteins. Furthermore, constituents of functional assemblies can aggregate and become non-functional during aging. Here we present the current knowledge as to how coalescing protein assemblies are spatially organized in cells and we postulate that failures in their spatial confinement might underscore certain aspects of aging and neurodegenerative diseases.en_US
dc.format.extent162 - 173en_US
dc.languageengen_US
dc.relation.ispartofPrionen_US
dc.rightsThis is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives License (http://creativecommons.org/licenses/by-nc-nd/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited, and is not altered, transformed, or built upon in any way.
dc.subjectAgingen_US
dc.subjectHumansen_US
dc.subjectMultiprotein Complexesen_US
dc.subjectNeurodegenerative Diseasesen_US
dc.subjectProteinsen_US
dc.subjectSaccharomyces cerevisiaeen_US
dc.titleSpatial regulation of coalesced protein assemblies: Lessons from yeast to diseases.en_US
dc.typeArticle
dc.rights.holder© 2017 The Author(s).
dc.identifier.doi10.1080/19336896.2017.1322239en_US
pubs.author-urlhttps://www.ncbi.nlm.nih.gov/pubmed/28574744en_US
pubs.issue3en_US
pubs.notesNo embargoen_US
pubs.notesOAen_US
pubs.organisational-group/Queen Mary University of London
pubs.organisational-group/Queen Mary University of London/Faculty of Science & Engineering
pubs.organisational-group/Queen Mary University of London/Faculty of Science & Engineering/Biological and Chemical Sciences - Staff
pubs.publication-statusPublisheden_US
pubs.volume11en_US


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