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dc.contributor.authorWilson, Kyleeng
dc.contributor.corporatenameUniversity of Missouri-Columbia. Office of Undergraduate Researcheng
dc.contributor.meetingnameSummer Undergraduate Research and Creative Achievements Forum (2004 : University of Missouri--Columbia)eng
dc.date.issued2004eng
dc.descriptionAbstract only availableeng
dc.description.abstractResident membrane proteins of the yeast trans-Golgi network (TGN) frequently cycle between the TGN and both the early and late (prevacuolar) endosomal compartments. The model yeast TGN protein, A-ALP, which contains the cytosolic domain of the TGN protein, depeptidyl aminopeptidase A (DPAP A), and the transmembrane and lumenal domains of the vacuolar membrane protein, alkaline phosphatase, have been studied. The cytosolic domain of A-ALP has been shown to be phosphorylated in vivo and in vitro. Of the 25 potentially phosphorylatable residues, only one, Ser13, was observed to influence trafficking between the TGN and endosomes. It has been suggested that phosphorylation of Ser13 is required for trafficking of A-ALP from the TGN to the pre-vacuolar compartment, which implies that phosphorylation of Ser13 may act as a switch for association of A-ALP with vesicular trafficking machinery. It is also important to note that once A-ALP reaches the vacuole by way of the PVC, it is cleaved in the lumenal domain, which allows us to follow the trafficking of the protein. We designed a screen to overexpress negative regulators, such as phosphatase, so that A-ALP will exhibit slower trafficking to the pre-vacuolar compartment. Yeast that seemed to have slower A-ALP trafficking to the PVC were identified by an ALP Overlay Assay. These positives are now being screened by western blot in order to verify that these cells exhibit slower trafficking to the PVC and eventually the vacuole. This can be determined by a western blot by examining the amount of processing of A-ALP in the vacuole. Those that are processed less give the indication of slower trafficking to the PVC, which is possibly the result of high phosphatase activity.eng
dc.description.sponsorshipLife Sciences Undergraduate Research Opportunity Programeng
dc.identifier.urihttp://hdl.handle.net/10355/2049eng
dc.languageen_USeng
dc.publisherUniversity of Missouri--Columbia. Office of Undergraduate Researcheng
dc.relation.ispartof2004 Summer Undergraduate Research and Creative Achievements Forum (MU)eng
dc.relation.ispartofcommunityUniversity of Missouri-Columbia. Office of Undergraduate Research. Undergraduate Research and Creative Achievements Forumeng
dc.source.urihttp://undergradresearch.missouri.edu/forums-conferences/abstracts/abstract-detail.php?abstractid=eng
dc.subjectyeasteng
dc.subjectyeast trans-Golgi networkeng
dc.subjectprevacuolar endosomal compartmentseng
dc.subjectresident membrane proteinseng
dc.subjectdepeptidyl aminopeptidase Aeng
dc.subjectalkaline phosphataseeng
dc.subjectphosphorylationeng
dc.subjectSer13eng
dc.titleA multicopy suppressor screen in yeast to look for negative regulators of Ser13 phosphorylation-based trafficking to the pre-vacuolar compartmenteng
dc.typePresentationeng


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