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dc.identifier.urihttp://hdl.handle.net/1951/55348
dc.identifier.urihttp://hdl.handle.net/11401/70925
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.typeDissertation
dcterms.abstractMammalian inositol-specific phospholipase Cβ1 (PLCβ1) is activated by Gαq subunits on the plasma membrane where it catalyzes hydrolysis of the minor membrane phosphatidylinositol 4,5 bisphosphate. While PLCβ1 localizes primarily to the plasma membrane it also exists in other compartments of the cell. It is not currently known what function PLCβ1 has in the cytosol and nucleus nor is it known what factors localize PLCβ1 to these compartments. In this study, we have identified a novel binding partner, translin-associated factor X (TRAX). Our experiments show that both proteins interact in solution and in cells. While TRAX exerts little effect on the membrane binding of PLCβ1, it does reduce the affinity of PLCβ1 for Gαq and inhibits the stimulation of PLCβ1 activity by Gαq. TRAX, a cytosolic protein that can localize to the nucleus, isinvolved in the down-regulation of protein expression by RNA interference. Our study shows that cytosolic PLCβ1 can drive TRAX out of the nucleus and reduce siRNA activity. Furthermore, activation of Gαq results in apparent displacement of cytosolic PLCβ1 from TRAX and concurrently allows TRAX to relocalize to the nucleus. Importantly we have found that increased cytosolic expression of PLCβ1 appears to reverse the siRNA-induced down-regulation of GAPDH. Our data suggests a potential link between Gαq activation, PLCβ1 localization and siRNA activity.
dcterms.available2012-05-15T18:02:00Z
dcterms.available2015-04-24T14:45:08Z
dcterms.contributorNicole Sampsonen_US
dcterms.contributorScarlata, Suzanneen_US
dcterms.contributorLondon, Erwinen_US
dcterms.contributorMario Rebecchien_US
dcterms.contributorDavid F. Green.en_US
dcterms.creatorAisiku, Omozuanvbo Reginald
dcterms.dateAccepted2012-05-15T18:02:00Z
dcterms.dateAccepted2015-04-24T14:45:08Z
dcterms.dateSubmitted2012-05-15T18:02:00Z
dcterms.dateSubmitted2015-04-24T14:45:08Z
dcterms.descriptionDepartment of Biochemistry and Structural Biologyen_US
dcterms.formatMonograph
dcterms.formatApplication/PDFen_US
dcterms.identifierhttp://hdl.handle.net/1951/55348
dcterms.identifierAisiku_grad.sunysb_0771E_10308.pdfen_US
dcterms.identifierhttp://hdl.handle.net/11401/70925
dcterms.issued2010-12-01
dcterms.languageen_US
dcterms.provenanceMade available in DSpace on 2012-05-15T18:02:00Z (GMT). No. of bitstreams: 1 Aisiku_grad.sunysb_0771E_10308.pdf: 13613937 bytes, checksum: 27ded43d2f045a029a6ee99121a22b51 (MD5) Previous issue date: 1en
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dcterms.publisherThe Graduate School, Stony Brook University: Stony Brook, NY.
dcterms.subjectBiophysics _ Cellular Biology
dcterms.subjectCell Biology, FRET, G protein, Phospholipase C, RNA
dcterms.titleThe Identification of a Novel Binding Partner for Phospholipase Cβ1, Translin-¶ðAssociated Factor X: A Link to ¶ÿRNA Interference
dcterms.typeDissertation


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