Publikationsserver der Universitätsbibliothek Marburg
Titel:Der Arf-GEF Schizo fördert die Fusion der Myoblasten über die Aktivierung der D-Arf1-GTPase während der frühen Myogenese von Drosophila melanogaster, während der Arf-GAP D-Git in Kooperation mit D-Arf6 die Wegfindung der Muskeln in der späten Myogenese beeinflusst
Autor:Dottermusch, Christine
Weitere Beteiligte: Önel, Susanne-Filiz (Prof. Dr.)
Veröffentlicht:2011
URI:https://archiv.ub.uni-marburg.de/diss/z2011/0495
DOI: https://doi.org/10.17192/z2011.0495
URN: urn:nbn:de:hebis:04-z2011-04959
DDC: Biowissenschaften, Biologie
Titel (trans.):The Arf-GEF Schizo directs myoblast fusion through activation of the D-Arf1 GTPase, whereas the Arf-GAP D-Git controls targeting of muscles cooperating with the D-Arf6 GTPase
Publikationsdatum:2011-09-06
Lizenz:https://rightsstatements.org/vocab/InC-NC/1.0/

Dokument

Schlagwörter:
Muskelentwicklung, Developmental Biology, Entwicklungsbiologie, Taufliege, myogenesis

Zusammenfassung:
In Drosophila melanogaster entstehen die mehrkernigen Muskeln der Körperwandmuskulatur durch die heterologe Fusion von Founderzellen (FCs) und Fusions-kompetenten Myoblasten (FCMs). Mutanten für das Gen schizo weisen nur unfusionierte Myoblasten auf, was auf eine essentielle Funktion dieses Gens für den Fusionsprozess hinweist. Zelltyp-spezifische Rettungsexperimente konnten zeigen, dass Schizo sowohl in FCs als auch in FCMs benötigt wird. Schizo kodiert für einen Guanin-Nukleotid-Austauschfaktor (GEF), welcher den GDP/GTP-Austausch an Arf-GTPasen katalysiert. Ein Ziel dieser Arbeit war es daher, zu analysieren, welche der Drosophila Arf-GTPasen, D-Arf1, D-Arf2 oder D-Arf6, während der Myoblastenfusion von Schizo aktiviert wird. Anders als das Vertebraten Homolog Brag2 scheint Schizo die Myoblastenfusion über die Aktivierung der D Arf1-GTPase und nicht der D-Arf6-GTPase zu fördern, da die Einführung der aktivierten Form von D-Arf1 eine partielle Rettung des schizo induzierten Fusionsdefekt bewirkte. Diese Vermutung wird zudem durch Hefe-Zwei-Hybrid-Daten unterstützt, in denen eine Interaktion zwischen Schizo und der GDP-gebundenen Form beobachtet werden konnte. Jedoch resultierte der Verlust der D-Arf1-Aktivität nicht in Fusionsstörungen. Dies könnte durch die maternal bereitgestellte mRNA von d-arf1 oder durch eine funktionelle Redundanz mit D-Arf2 begründet sein, da eine funktionelle Redundanz mit D Arf6 ausgeschlossen werden konnte. Genetische Interaktionsstudien und Rettungsexperimente mit bekannten Aktin-Regulatoren widerlegen zudem die Vermutung von Chen et al. (2003), dass Schizo über die Lokalisation der Rac-GTPase an der Umstrukturierung des Aktin-Zytoskeletts beteiligt ist und stehen im Einklang damit, dass Schizo ein GEF für D-Arf1 ist. Des Weiteren wurde das mRNA Verteilungsmuster von Drosophila Arf-GTPase-aktivierende Proteinen (Arf-GAPs) untersucht, die möglicherweise an der Hydrolyse des D-Arf1-GTP während der Myoblastenfusion beteiligt sein könnten. Unter diesen konnte das Drosophila Homolog von Git1, D Git, als im Mesoderm angereicherter Arf-GAP identifiziert werden. Die in dieser Arbeit erfolgreich generierten Mutanten für d-git zeigen zwar keine Fusionsdefekte, weisen jedoch Fehler in der Wegfindung und Morphogenese insbesondere der ventralen Muskeln auf. Während der Wegfindung strecken sich mehrkernige Muskeln in Richtung ihrer epidermalen Anheftungsstelle, wobei sie an ihren Enden Aktin-reiche Filopodien ausbilden, welche die Umgebung auf leitende Signale absuchen. In Übereinstimmung mit einer Funktion von D-Git in den späten Aspekten der Muskelentwicklung befindet sich das D-Git Protein konzentriert an den Enden der wachsenden Muskeln. Interaktions- und Lokalisationsstudien mit dem Adhäsions-assoziiertem Protein Paxillin zeigen, dass die Wegfindung der Muskeln nicht mit der Integrin-vermittelten Adhäsion der Muskeln gekoppelt ist. Genetische Interaktionsstudien konnten jedoch belegen, dass D-Git während der Wegfindung der Muskeln mit der D-Arf6-GTPase kooperiert, wodurch es wahrscheinlich externe Wegfindungssignale auf das Aktin-Zytoskelett und/oder den Membrantransport in den Enden der Muskeln überträgt.

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