Publikationsserver der Universitätsbibliothek Marburg

Titel:Charakterisierung der Lokalisation von Prestin (SLC26A5) in Membran-Mikrodomänen
Autor:Feuer, Anja
Weitere Beteiligte: Oliver, Dominik (Prof. Dr.)
Veröffentlicht:2016
URI:https://archiv.ub.uni-marburg.de/diss/z2017/0144
URN: urn:nbn:de:hebis:04-z2017-01448
DOI: https://doi.org/10.17192/z2017.0144
DDC: Biowissenschaften, Biologie
Titel (trans.):Characterisation of localisation of Prestin (SLC26A5) in membran microdomains
Publikationsdatum:2017-02-23
Lizenz:https://creativecommons.org/licenses/by-nc-sa/4.0

Dokument

Schlagwörter:
Cytoskeleton, Mikrodomänen, Zytoskelett, Prestin, Prestin, Prestin, Äußere Haarzellen, Outer Haircells, Microdomains, Caveolin, Caveolin

Zusammenfassung:
Prestin (SLC26A5; Pres) nimmt eine Schlüsselstellung für die Funktion des SäugetierInnenohres ein. Es ist das Motorprotein der ÄHZ (Zheng et al. 2000), welches in Antwort auf Änderungen des Membranpotenzials ultraschnelle Längenänderungen der ÄHZ generiert (Brownell et al. 1985). Es wird angenommen, dass dieser als Elektromotilität bezeichnete Vorgang die Grundlage des elektro-mechanischen Verstärkerprozesses der ÄHZ darstellt und für die außerordentliche Sensitivität des Gehörs sorgt (Liberman et al. 2002). Der Verlust des Verstärkermechanismus der ÄHZ ist die häufigste Ursache von Schwerhörigkeit beim Menschen. Immunolokalisationen von nativem Pres zeigen eine subzelluläre Lokalisation in der lateralen Plasmamembran der ÄHZ (Winter et al. 2006). Die vorliegende Arbeit charakterisiert mittels verschiedener hoch auflösender FluoreszenzMikroskopie-Techniken die spezifische subzelluläre Lokalisation der Pres-Orthologen aus Wanderratte (Rattus norvegicus; rPres), Zebrafisch (Danio rerio; zPres) und Huhn (Gallus gallus; cPres) im heterologen Expressionssystem. Alle Pres-Orthologen offenbarten eine plasmamembran-ständige Lokalisation, jedoch Unterschiede in der Membran-Verteilung. Pres-Proteine aus Huhn wiesen eine homogene Verteilung auf. Die Orthologen aus Zebrafisch und Wanderratte hingegen lokalisierten als mikroskopisch sichtbare, fokale Cluster. Als eine molekulare Determinante dieser differenziellen Lokalisation wurde die TransmembranDomäne (TMD) von Pres identifiziert, d.h., die intrinsischen Eigenschaften der TMD sind für das Verteilungsverhalten von Pres ursächlich. Weiterhin wurde herausgefunden, dass die biophysikalischen Bedingungen der Plasmamembran das Clustering ebenfalls beeinflussen: So wurde gezeigt, dass die Verteilung von Pres vom Cholesterol-Gehalt der Zellen und der Temperatur abhängig ist. Darüber hinaus wird die Verteilung von Pres durch Proteine mitbestimmt. Das mikrodomänenassoziierte Cav-1 ko-lokalisierte mit Pres und induzierte einerseits das Clustering von cPres, war andererseits aber für die Lokalisation als Cluster nicht essentiell. Das Pres-Clustering war eng mit dem Zytoskelett assoziiert. So ko-lokalisierten Aktin- wie auch Map1S-Punkte mit den Pres-Clustern. Eine Depolymerisation des Aktin-Zytoskeletts löste die Cluster partiell auf. Heterolog exprimiertes Map1S verhinderte diese Auflösung. Biochemisch wurde abschließend gezeigt, dass Aktin und Cav-1 mit Pres cholesterol-abhängig interagieren. Zusammenfassend liegt Pres bei heterologer Expression in cholesterol-reichen und zytoskelettabhängigen lipid-raft-artigen Membran-Domänen als Protein-Komplex mit Cav-1, Aktin und Map1S vor. Die vorliegende Arbeit ermöglichte es, molekularen Eigenschaften der Pres-Membran-Domäne zu identifizieren und zeigt Kandidaten auf, die das Motorprotein der ÄHZ in der lateralen Membran organisieren könnten. Diese Kandidaten können an der Regulation der Elektromotilität beteiligt sein.

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