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Conserved roles of the prion protein domains on subcellular localization and cell-cell adhesion

Conserved roles of the prion protein domains on subcellular localization and cell-cell adhesion

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Prüfsumme: MD5:398c94712f627da1b8f03a5ba0bb63f0

SOLIS, Gonzalo P, Yvonne RADON, Aimilia SEMPOU, Katharina JECHOW, Claudia STÜRMER, Edward MÁLAGA TRILLO, 2013. Conserved roles of the prion protein domains on subcellular localization and cell-cell adhesion. In: PLoS ONE. 8(7), e70327. eISSN 1932-6203

@article{Solis2013Conse-24316, title={Conserved roles of the prion protein domains on subcellular localization and cell-cell adhesion}, year={2013}, doi={10.1371/journal.pone.0070327}, number={7}, volume={8}, journal={PLoS ONE}, author={Solis, Gonzalo P and Radon, Yvonne and Sempou, Aimilia and Jechow, Katharina and Stürmer, Claudia and Málaga Trillo, Edward}, note={Article Number: e70327} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/24316"> <dcterms:bibliographicCitation>PLoS One ; 8 (2013), 7. - e70327</dcterms:bibliographicCitation> <dc:creator>Sempou, Aimilia</dc:creator> <dc:creator>Solis, Gonzalo P</dc:creator> <dc:creator>Radon, Yvonne</dc:creator> <dc:contributor>Jechow, Katharina</dc:contributor> <dcterms:issued>2013</dcterms:issued> <dc:contributor>Sempou, Aimilia</dc:contributor> <dc:creator>Stürmer, Claudia</dc:creator> <dc:creator>Jechow, Katharina</dc:creator> <dcterms:title>Conserved roles of the prion protein domains on subcellular localization and cell-cell adhesion</dcterms:title> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2013-08-23T12:40:51Z</dc:date> <dc:language>eng</dc:language> <dc:contributor>Radon, Yvonne</dc:contributor> <dc:rights>deposit-license</dc:rights> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/24316"/> <dc:contributor>Málaga Trillo, Edward</dc:contributor> <dc:contributor>Solis, Gonzalo P</dc:contributor> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2013-08-23T12:40:51Z</dcterms:available> <dcterms:rights rdf:resource="http://nbn-resolving.org/urn:nbn:de:bsz:352-20140905103605204-4002607-1"/> <dc:creator>Málaga Trillo, Edward</dc:creator> <dc:contributor>Stürmer, Claudia</dc:contributor> <dcterms:abstract xml:lang="eng">Analyses of cultured cells and transgenic mice expressing prion protein (PrP) deletion mutants have revealed that some properties of PrP -such as its ability to misfold, aggregate and trigger neurotoxicity- are controlled by discrete molecular determinants within its protein domains. Although the contributions of these determinants to PrP biosynthesis and turnover are relatively well characterized, it is still unclear how they modulate cellular functions of PrP. To address this question, we used two defined activities of PrP as functional readouts: 1) the recruitment of PrP to cell-cell contacts in Drosophila S2 and human MCF-7 epithelial cells, and 2) the induction of PrP embryonic loss- and gain-of-function phenotypes in zebrafish. Our results show that homologous mutations in mouse and zebrafish PrPs similarly affect their subcellular localization patterns as well as their in vitro and in vivo activities. Among PrP's essential features, the N-terminal leader peptide was sufficient to drive targeting of our constructs to cell contact sites, whereas lack of GPI-anchoring and N-glycosylation rendered them inactive by blocking their cell surface expression. Importantly, our data suggest that the ability of PrP to homophilically trans-interact and elicit intracellular signaling is primarily encoded in its globular domain, and modulated by its repetitive domain. Thus, while the latter induces the local accumulation of PrPs at discrete punctae along cell contacts, the former counteracts this effect by promoting the continuous distribution of PrP. In early zebrafish embryos, deletion of either domain significantly impaired PrP's ability to modulate E-cadherin cell adhesion. Altogether, these experiments relate structural features of PrP to its subcellular distribution and in vivo activity. Furthermore, they show that despite their large evolutionary history, the roles of PrP domains and posttranslational modifications are conserved between mouse and zebrafish.</dcterms:abstract> </rdf:Description> </rdf:RDF>

Dateiabrufe seit 01.10.2014 (Informationen über die Zugriffsstatistik)

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