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dc.identifier.urihttp://hdl.handle.net/11401/76886
dc.description.sponsorshipThis work is sponsored by the Stony Brook University Graduate School in compliance with the requirements for completion of degree.en_US
dc.formatMonograph
dc.format.mediumElectronic Resourceen_US
dc.language.isoen_US
dc.publisherThe Graduate School, Stony Brook University: Stony Brook, NY.
dc.typeThesis
dcterms.abstractSignal transduction relies on the proper localization of proteins to properly transfer signals throughout the cell. The cell membrane serves as a vital interface for the proper localization of proteins. Posttranslational modifications cause proteins to become targeted to membranes. One such modification is palmitoylation, the addition of a palmitic acid to a cysteine of a protein. Within the neuron, a large protein complex called the postsynaptic density receives upstream signals at the synapse. Many signaling proteins within the postsynaptic density are known to require palmitoylation for proper trafficking and function. Two such examples are the N-methyl-D-Aspartate receptor (NMDAR) and Post Synaptic Density Protein 95 (PSD95). While studies have been carried out on their soluble forms, their palmitoylated forms have not been well studied. This is due to the difficulty in palmitoylating proteins in-vitro. We circumvent this issue by utilizing phosphopantetheinyl transferases (PPTases) to palmitoyate proteins. PPTases are able to attach various Coenzyme A substrates to proteins with specific tag sequences. We also develop a 2-step assay to quantify the effectiveness of the palmitoylation reaction. We successfully show that palmitoylation using AcpS, a PPTase, is possible utilizing the developed assays.
dcterms.available2017-09-20T16:51:22Z
dcterms.contributorBowen, Mark Een_US
dcterms.contributorMiller, W. Todden_US
dcterms.creatorChang, Victor
dcterms.dateAccepted2017-09-20T16:51:22Z
dcterms.dateSubmitted2017-09-20T16:51:22Z
dcterms.descriptionDepartment of Biochemistry and Cell Biologyen_US
dcterms.extent47 pg.en_US
dcterms.formatMonograph
dcterms.formatApplication/PDFen_US
dcterms.identifierhttp://hdl.handle.net/11401/76886
dcterms.issued2016-12-01
dcterms.languageen_US
dcterms.provenanceMade available in DSpace on 2017-09-20T16:51:22Z (GMT). No. of bitstreams: 1 Chang_grad.sunysb_0771M_13162.pdf: 2734934 bytes, checksum: a1be2dce61fa5afd1acdd5d61f71323a (MD5) Previous issue date: 1en
dcterms.publisherThe Graduate School, Stony Brook University: Stony Brook, NY.
dcterms.subjectNMDAR, Palmitoylation, Phosphonatetheinyl Transferase, PPTase, PSD95
dcterms.subjectBiochemistry
dcterms.titlePalmitoylation of the NMDA receptor and PSD95 utilizing Phosphopantetheinyl Transferases
dcterms.typeThesis


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