Use this URL to cite or link to this record in EThOS: http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.630871
Title: The identification of a new molecular tool to investigate the role of actin and microtubule cytoskeletons in the endocytosis pathway of the pathogenic fungus Ustilago maydis
Author: Clark, Natalie
ISNI:       0000 0004 5354 209X
Awarding Body: University of Exeter
Current Institution: University of Exeter
Date of Award: 2014
Availability of Full Text:
Access through EThOS:
Access through Institution:
Abstract:
Endocytosis is essential for the pathogenic development of Ustilago maydis. It has been shown that the initiation of pathogenicity relies upon the ability of the cell to recognize pheromone (a1 or a2) released from its mating partner and subsequently to form conjugated hyphae. The actin and microtubule cytoskeleton plays an essential role in all aspects of cell growth. A component of the actin cytoskeleton, the filamentous actin is required for cell-cell fusion, whereas the molecular motors, kinesin and dynein, move along microtubules and provide the long distance transport of many proteins and they are important in cell growth and pathogenicity. In this thesis, we investigated the role of the cytoskeleton in endocytosis and a1 pheromone transport, using a fluorescently labelled derivative of the a1 pheromone. We confirmed that uptake of the a1 pheromone is also receptormediated. In addition, we have shown that pheromone transport towards the cellular vacuole requires the actin and microtubule cytoskeletons. Furthermore, we revealed that the microtubule-dependent motors kinesin-1 and kinesin-3 and dynein were shown to be essential in the delivery of the pheromone to vacuoles. Moreover, a mutation in the early endosomal protein Yup1 gene causes a stop in delivery of the synthetic pheromone to the vacuole. This suggests that it travels with early endosomes. Within the actin cytoskeleton, we analysed the dynamics of actin patches in the presence of the synthetic pheromone and found that the dynamics of the patches increased significantly. Additionally, in the presence of an over-expression of the tail domain of the molecular motor myosin-5, the dynamics of the patches were significantly reduced and their intensity diminished.
Supervisor: Wood, Mark; Steinberg, Gero Sponsor: BBSRC
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.630871  DOI: Not available
Keywords: Endocytosis ; Ustilago maydis ; Actin cytoskeleton ; Microtubule cytoskeleton ; Pheromone ; Receptors ; Myosin-5
Share: