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dc.contributor.authorAlotaibi, Dalal
dc.date.accessioned2019-11-28T15:12:26Z
dc.date.available2019-11-28T15:12:26Z
dc.date.issued2019-11-28T15:12:26Z
dc.identifier.urihttp://hdl.handle.net/10222/76671
dc.description.abstractUbiquitin Proteasome System (UPS) regulates the abundance of proteins by first attaching ubiquitin molecules and then targeting the modified protein for degradation by the 26S proteasome. E3 ubiquitin ligases are the central enzymes of the UPS that is responsible for selecting substrates for ubiquitination. The Arabidopsis thaliana E3 Keep on Going (KEG) was shown to negatively regulate the activity of the stress hormone abscisic acid (ABA) by ubiquitinating components of the hormone signaling network, including Calcineurin B-Like Interacting Protein Kinase 26 (CIPK26). This work investigates the role of the UPS in regulating CIPK proteins, specifically CIPK3, CIPK8, CIPK20, and CIPK24. We examine ubiquitination and the proteasome-dependent degradation of the selected CIPKs in the plant cell by using transient protein expression systems. All the examined CIPKs were found to be ubiquitinated in plant cells. Interestingly, we found that all but CIPK24, which is stable, are targeted for degradation by 26S proteasome.en_US
dc.subjectUbiquitin Proteasome Systemen_US
dc.subjectCalcineurin B-Like Interacting Protein Kinase (CIPK)en_US
dc.titleRegulation of Arabidopsis thaliana Calcineurin B-like Interacting Protein Kinases (CIPKs) by the Ubiquitin-Proteasome Systemen_US
dc.date.defence2017-04-18
dc.contributor.departmentDepartment of Biologyen_US
dc.contributor.degreeMaster of Scienceen_US
dc.contributor.external-examinern/aen_US
dc.contributor.graduate-coordinatorDr. Sophia Stoneen_US
dc.contributor.thesis-readerDr. Mirwais Qaderien_US
dc.contributor.thesis-readerDr. Balakrishnan Prithivirajen_US
dc.contributor.thesis-supervisorDr. Sophia Stoneen_US
dc.contributor.ethics-approvalNot Applicableen_US
dc.contributor.manuscriptsNot Applicableen_US
dc.contributor.copyright-releaseNot Applicableen_US
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