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dc.contributor.advisorNothwehr, Steven F.eng
dc.contributor.authorFoote, Christopher, 1970-eng
dc.date.issued2005eng
dc.date.submitted2005 Falleng
dc.descriptionThe entire dissertation/thesis text is included in the research.pdf file; the official abstract appears in the short.pdf file (which also appears in the research.pdf); a non-technical general description, or public abstract, appears in the public.pdf file.eng
dc.descriptionTitle from title screen of research.pdf file viewed on (November 7, 2006)eng
dc.descriptionIncludes bibliographical references.eng
dc.descriptionVita.eng
dc.descriptionThesis (Ph. D.) University of Missouri-Columbia 2005.eng
dc.descriptionDissertations, Academic -- University of Missouri--Columbia -- Biological sciences.eng
dc.description.abstractIn Saccharomyces cerevisiae it is generally accepted that there are two routes for trafficking of proteins from the trans-Golgi network (TGN) to the vacuole. One involves direct transport from the TGN to the vacuole. The second involves transport from the TGN to the prevacuolar compartment (PVC) via GGA coated vesicles, followed by PVC to vacuole transport. We propose that there is a third route. This route entails transit from the TGN to the early endosome (EE), followed by delivery to the PVC and vacuole. In support of an alternative route, the processing kinetics of A(F[arrow]A)-ALP are not affected by mutations in the GGA proteins. This is in contrast to proteins that use the GGA pathway, as their delivery to the vacuole is significantly slowed when GGA function is ablated. Further support of an EE itinerary is the observation that A(F[arrow]A)-ALP co localizes with the lipophilic dye, FM4-64 at a time when the dye is associated with the EE. Disruption of the AP-1 vesicle coat complex leads to an accelerated processing of A(F[arrow]A)-ALP. Appending the region of A(F[arrow]A)-ALP that interacts with AP-1 to Cps1p delays its progress to the vacuole. These results are consistent with a model in which A(F[arrow]A)-ALP passes through the EE in transit to the vacuole. A(F[arrow]A)-ALP physically interacts with AP-1, and this interaction delays its delivery to the vacuole. Data presented in this thesis suggests that in Saccharomyces cerevisiae AP-1 functions as a retrieval mechanism from the EE to the TGN.eng
dc.identifier.merlinb57087568eng
dc.identifier.urihttps://hdl.handle.net/10355/4172
dc.identifier.urihttps://doi.org/10.32469/10355/4172eng
dc.languageEnglisheng
dc.publisherUniversity of Missouri--Columbiaeng
dc.relation.ispartofcommunityUniversity of Missouri--Columbia. Graduate School. Theses and Dissertationseng
dc.sourceSubmitted by University of Missouri--Columbia Graduate School.eng
dc.subject.lcshEndosomeseng
dc.subject.lcshSaccharomyces cerevisiaeeng
dc.subject.lcshGolgi apparatuseng
dc.subject.lcshCarrier proteinseng
dc.titleThe role of the AP-1 adaptor complex in trafficking between the trans-Golgi Network and endosomal systemeng
dc.typeThesiseng
thesis.degree.disciplineBiological sciences (MU)eng
thesis.degree.grantorUniversity of Missouri--Columbiaeng
thesis.degree.levelDoctoraleng
thesis.degree.namePh. D.eng


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