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Identification of phosphorylation sites of TOPORS and a role for phosphorylated residues in the regulation of ubiquitin and SUMO E3 ligase activity
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Park, Hye-Jin. Identification of phosphorylation sites of TOPORS and a role for phosphorylated residues in the regulation of ubiquitin and SUMO E3 ligase activity. Retrieved from https://doi.org/doi:10.7282/T3HQ403V

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TitleIdentification of phosphorylation sites of TOPORS and a role for phosphorylated residues in the regulation of ubiquitin and SUMO E3 ligase activity
NamePark, Hye-Jin (author); Rubin, Eric (chair); Suh, Nanjoo (internal member); Chen, Suzie (internal member); Kim, Isaac (outside member); Rutgers University; Graduate School - New Brunswick
Date Created
Other Date2008-10 (degree)
SubjectPharmaceutical Science, DNA topoisomerases, Phosphorylation, Ubiquitin, Ligases
Extentvii, 108 p. : ill.
DescriptionTOPORS is the first example of a protein that possesses both ubiquitin and SUMO E3 ligase activity. The ubiquitination activity maps to a conserved RING domain in the N-terminal region of the protein, which is not required for sumoylation activity. Similar to other E3 ligases, it is likely that the ubiquitin and sumoylation activities of TOPORS are regulated by post-translational modifications. Therefore, we employed mass spectrometry to identify post-translational modifications of TOPORS. Several putative phosphorylated regions were identified in conserved regions of the protein. We investigated the role of phosphorylation of serine 98, which is adjacent to the RING domain, in both cells and in vitro. Mutation of serine 98 to aspartic acid resulted in an increase in the ubiquitin ligase activity of TOPORS both in cells and in vitro. In addition, this mutation increased the binding of TOPORS to the E2 enzyme UbcH5a. Conversely, a phospho-deficient mutant (S98A) exhibited little change in ubiquitin ligase activity compared to wild-type TOPORS, both in cells and in vitro. Neither of the mutants affected the localization of TOPORS to punctate nuclear regions. In addition, neither mutant affected the SUMO ligase activity of TOPORS in cells or in vitro. Our findings indicate that phosphorylation of serine 98 regulates the ubiquitin but not the SUMO ligase activity of TOPORS, consistent with a potential binary switch function for TOPORS in protein ubiquitination versus sumoylation.
NotePh.D.
NoteIncludes bibliographical references (p. 99-107)
Noteby Hye-Jin Park
Genretheses, ETD doctoral
Persistent URLhttps://doi.org/doi:10.7282/T3HQ403V
Languageeng
CollectionGraduate School - New Brunswick Electronic Theses and Dissertations
Organization NameRutgers, The State University of New Jersey
RightsThe author owns the copyright to this work.
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