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dc.contributor.advisorArturo De Lozanneen
dc.creatorCaffarelli, Nicolasen
dc.date.accessioned2011-09-02T15:26:53Zen
dc.date.available2011-09-02T15:26:53Zen
dc.date.created2009en
dc.date.issued2011-09-02en
dc.identifier.urihttp://hdl.handle.net/2152/13384en
dc.description.abstractIn order for cells to eat, they must detect food at their cell surface and pull it in to form a vesicle known as an endosome. This endosome then becomes acidified to become a lysosome and eventually becomes neutral again, as a postlysosome, so that waste can be expelled from the cell. Collectively, this is referred to as the endocytic pathway. Several proteins are involved in this process – Rabs are known to mediate specificity of fusing vesicles, and SNARES catalyze the actual vesicle fusion. In this study we look at the protein Vps33, a subunit of the HOPS complex. The HOPS complex is known to interact with Rabs and SNARES, and we are interested as to where it acts within the cell. By tagging Vps33 with Green Fluorescent Protein (GFP), we can visualize its localization under the microscope. We observe here that Vps33 localizes primarily to the cytoplasm, with sparse localization to intracellular vesicles.en
dc.language.isoengen
dc.subjectCollege of Natural Sciencesen
dc.subjectendocytic pathwayen
dc.subjectproteinsen
dc.subjectVps33en
dc.subjectHOPS complexen
dc.subjectRabsen
dc.subjectSNARESen
dc.titleThe HOPS complex and Vps33 in Dictyostelium discoideumen
dc.typeThesisen
dc.description.departmentBiological Sciences, School ofen


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