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dc.contributor.advisorGiordano, Antonio
dc.creatorMarsili, Stefania
dc.date.accessioned2020-10-27T15:27:41Z
dc.date.available2020-10-27T15:27:41Z
dc.date.issued2011
dc.identifier.other864885315
dc.identifier.urihttp://hdl.handle.net/20.500.12613/1837
dc.description.abstractA convincing body of evidence suggests that ubiquitination and the ubiquitin proteasome degradation pathway play a key role in neoplastic transformation. Ubiquitination, as post-translation modification, is involved both in functional regulation and degradation of specific cellular targets known as proto-oncogenes and tumor suppressors. Oncogenic viral proteins interact both with proto-oncoproteins and tumor suppressors leading to the modulation of their cellular function by several mechanisms including ubiquitination. Interestingly, viral oncoproteins themselves can also be regulated by this post-translation modification. Additionally, viruses can assemble their own E3 ligases or regulate the activity of cellular E3 ligases. E3 ligases, involved in the final step of the ubiquitination process, are the enzymes that provide the specificity for the interaction with target substrates by the means of a large number of proteins. Recent studies on the potential correlation between viral infection and oncogenesis, have addressed the emerging role of the ubiquitination system as a possible mediator for cancer transformation. In this scenario we hypothesized that JCV T-antigen may interfere with the ubiquitination system and we investigated a possible interaction between JCV T-antigen and the E3 ligase Cul7. To prove our hypothesis we performed co-immunoprecipitation and co-immunofluorescence experiments using the glioblastoma cell lines HJC12, U87MG and HJC5. Our results indicate that JCV T-antigen and Cul7 interact in the cytoplasmic compartment. In addition, JCV T-antigen stabilizes Cul7. These observations suggest that JCV T-antigen can modulate Cul7 E3 ligase activity leading to oncogenesis. Further study addressing the biological significance of this interaction will decipher the cellular processes modulated by JCV T-antigen and Cul7 and will indicate new avenues for therapeutic intervention.
dc.format.extent59 pages
dc.language.isoeng
dc.publisherTemple University. Libraries
dc.relation.ispartofTheses and Dissertations
dc.rightsIN COPYRIGHT- This Rights Statement can be used for an Item that is in copyright. Using this statement implies that the organization making this Item available has determined that the Item is in copyright and either is the rights-holder, has obtained permission from the rights-holder(s) to make their Work(s) available, or makes the Item available under an exception or limitation to copyright (including Fair Use) that entitles it to make the Item available.
dc.rights.urihttp://rightsstatements.org/vocab/InC/1.0/
dc.subjectBiology
dc.subjectCellular Biology
dc.subjectNeurosciences
dc.subjectBrain
dc.subjectCancer
dc.subjectCul7
dc.subjectJcv
dc.subjectT-antigen
dc.subjectUbiquitination
dc.titleInterplay between JCV Large T-antigen and Cullin-7 in Brain Cancer
dc.typeText
dc.type.genreThesis/Dissertation
dc.contributor.committeememberKhalili, Kamel
dc.contributor.committeememberTuszynski, George P.
dc.contributor.committeememberWhite, Martyn K.
dc.description.departmentBiology
dc.relation.doihttp://dx.doi.org/10.34944/dspace/1819
dc.ada.noteFor Americans with Disabilities Act (ADA) accommodation, including help with reading this content, please contact scholarshare@temple.edu
dc.description.degreePh.D.
refterms.dateFOA2020-10-27T15:27:41Z


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