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000136874 0247_ $$2doi$$a10.1073/pnas.1217321110
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000136874 041__ $$aEnglish
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000136874 1001_ $$0P:(DE-2719)2630357$$aHofmann, Julia P$$b0$$eFirst author
000136874 245__ $$aCell-to-cell propagation of infectious cytosolic protein aggregates.
000136874 260__ $$aWashington, DC$$bNational Acad. of Sciences$$c2013
000136874 264_1 $$2Crossref$$3online$$bProceedings of the National Academy of Sciences$$c2013-03-18
000136874 264_1 $$2Crossref$$3print$$bProceedings of the National Academy of Sciences$$c2013-04-09
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000136874 520__ $$aPrions are self-templating protein conformers that replicate by recruitment and conversion of homotypic proteins into growing protein aggregates. Originally identified as causative agents of transmissible spongiform encephalopathies, increasing evidence now suggests that prion-like phenomena are more common in nature than previously anticipated. In contrast to fungal prions that replicate in the cytoplasm, propagation of mammalian prions derived from the precursor protein PrP is confined to the cell membrane or endocytic vesicles. Here we demonstrate that cytosolic protein aggregates can also behave as infectious entities in mammalian cells. When expressed in the mammalian cytosol, protein aggregates derived from the prion domain NM of yeast translation termination factor Sup35 persistently propagate and invade neighboring cells, thereby inducing a self-perpetuating aggregation state of NM. Cell contact is required for efficient infection. Aggregates can also be induced in primary astrocytes, neurons, and organotypic cultures, demonstrating that this phenomenon is not specific to immortalized cells. Our data have important implications for understanding prion-like phenomena of protein aggregates associated with human diseases and for the growing number of amyloidogenic proteins discovered in mammals.
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000136874 650_7 $$2NLM Chemicals$$aPeptide Termination Factors
000136874 650_7 $$2NLM Chemicals$$aPrions
000136874 650_7 $$2NLM Chemicals$$aSUP35 protein, S cerevisiae
000136874 650_7 $$2NLM Chemicals$$aSaccharomyces cerevisiae Proteins
000136874 650_7 $$0147336-22-9$$2NLM Chemicals$$aGreen Fluorescent Proteins
000136874 650_2 $$2MeSH$$aAnimals
000136874 650_2 $$2MeSH$$aAstrocytes: cytology
000136874 650_2 $$2MeSH$$aCell Communication
000136874 650_2 $$2MeSH$$aCoculture Techniques
000136874 650_2 $$2MeSH$$aCytoplasm: metabolism
000136874 650_2 $$2MeSH$$aCytosol: metabolism
000136874 650_2 $$2MeSH$$aGreen Fluorescent Proteins: metabolism
000136874 650_2 $$2MeSH$$aHippocampus: metabolism
000136874 650_2 $$2MeSH$$aMice
000136874 650_2 $$2MeSH$$aMicroscopy, Confocal
000136874 650_2 $$2MeSH$$aPeptide Termination Factors: metabolism
000136874 650_2 $$2MeSH$$aPrion Diseases
000136874 650_2 $$2MeSH$$aPrions: metabolism
000136874 650_2 $$2MeSH$$aProtein Conformation
000136874 650_2 $$2MeSH$$aSaccharomyces cerevisiae: metabolism
000136874 650_2 $$2MeSH$$aSaccharomyces cerevisiae Proteins: metabolism
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000136874 7001_ $$0P:(DE-2719)2810245$$aDenner, Philip$$b1
000136874 7001_ $$0P:(DE-HGF)0$$aNussbaum-Krammer, Carmen$$b2
000136874 7001_ $$0P:(DE-2719)2810327$$aKuhn, Peer-Hendrik$$b3
000136874 7001_ $$0P:(DE-HGF)0$$aSuhre, Michael H$$b4
000136874 7001_ $$0P:(DE-HGF)0$$aScheibel, Thomas$$b5
000136874 7001_ $$0P:(DE-2719)2181459$$aLichtenthaler, Stefan F$$b6
000136874 7001_ $$0P:(DE-HGF)0$$aSchätzl, Hermann M$$b7
000136874 7001_ $$0P:(DE-2719)2158358$$aBano, Daniele$$b8
000136874 7001_ $$0P:(DE-2719)2481765$$aVorberg, Ina M$$b9$$eLast author
000136874 77318 $$2Crossref$$3journal-article$$a10.1073/pnas.1217321110$$b : Proceedings of the National Academy of Sciences, 2013-03-18$$n15$$p5951-5956$$tProceedings of the National Academy of Sciences$$v110$$x0027-8424$$y2013
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