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dc.contributor.advisorFujita, Donald J.
dc.contributor.authorBabic, Ivan
dc.date.accessioned2005-08-16T17:08:55Z
dc.date.available2005-08-16T17:08:55Z
dc.date.issued2004
dc.identifier.citationBabic, I. (2004). Post-translational modifications regulating the activity of Sam68 (Unpublished doctoral thesis). University of Calgary, Calgary, AB. doi:10.11575/PRISM/20048en_US
dc.identifier.isbn049404585Xen
dc.identifier.urihttp://hdl.handle.net/1880/41717
dc.descriptionBibliography: p. 211-234en
dc.description.abstractSrc-associated in mitosis 68 kDa (Sam68) is an RNA binding protein identified 10 years ago as a mitosis specific target for Src tyrosine kinase. It belongs to the signal transduction and activation of RNA metabolism (STAR) protein family. These proteins are thought to link signaling pathways with some aspect of RNA metabolism. Although the function of Sam68 is unknown it has been reported to play a role in several biological processes such as: viral replication, cell signaling, alternative pre-mRNA splicing, cell cycle regulation, and has been suggested to be a tumour suppressor and a transcriptional regulator. It has been demonstrated that the activity of Sam68 can be regulated by post-translational modifications such as tyrosine or serine/threonine phosphorylation. Tyrosine phosphorylation was shown to inhibit Sam68 binding to synthetic poly(U) RNA, and serine/threonine phosphorylation was shown to influence the ability of Sam68 to alter splice site selection. Since Sam68 is predominantly a nuclear protein there are several post-translational modifications common to nuclear proteins that have not yet been described for Sam68. For example, acetylation, sumoylation and ubquitination are three post-translational modifications described for numerous nuclear proteins. Here I report that Sam68 can be acetylated, and that acetylation positively regulates its binding to poly(U) RNA. As well, Sam68 is shown to be sumoylated. Conjugation with SUMO altered Sam68 subnuclear localization and its ability to act asen
dc.format.extentxx, 234 leaves : ill. ; 30 cm.en
dc.language.isoeng
dc.rightsUniversity of Calgary graduate students retain copyright ownership and moral rights for their thesis. You may use this material in any way that is permitted by the Copyright Act or through licensing that has been assigned to the document. For uses that are not allowable under copyright legislation or licensing, you are required to seek permission.
dc.titlePost-translational modifications regulating the activity of Sam68
dc.typedoctoral thesis
dc.publisher.institutionUniversity of Calgaryen
dc.identifier.doihttp://dx.doi.org/10.11575/PRISM/20048
thesis.degree.nameDoctor of Philosophy
thesis.degree.namePhD
thesis.degree.disciplineBiochemistry and Molecular Biology
thesis.degree.grantorUniversity of Calgary
dc.identifier.lccAC1 .T484 2004 B325en
dc.publisher.placeCalgaryen
ucalgary.thesis.notesUARCen
ucalgary.thesis.uarcreleaseyen
ucalgary.item.requestcopytrue
ucalgary.thesis.accessionTheses Collection 58.002:Box 1487 520492004


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University of Calgary graduate students retain copyright ownership and moral rights for their thesis. You may use this material in any way that is permitted by the Copyright Act or through licensing that has been assigned to the document. For uses that are not allowable under copyright legislation or licensing, you are required to seek permission.