Details
- Close date
- No date set
- Academic background
- Health Sciences
- Host campus
- Dunedin
- Qualification
- PhD
- Department
- Pathology (Dunedin)
- Supervisor
- Dr Adele Woolley
Overview
Recdently published data suggests that the dynamic postranslational modification (PTM) of specific residues in YB-1 acts as a switch to assemble and disassemble SGs.
We have developed stable cell lines with a fluorescent label on YB-1 so that we can visualise the cellular location of YB-1 in real-time and can therefore monitor the formation and disassembly of SGs.
We will also investigate specific kinases that are involved in this dynamic PTM of YB-1, using genetically-encoded fluorescent FRET kinase biosensors.
Useful information
Similar research opportunities
- Characterisation of YB-1 interactions with the cytoskeleton using live cell imaging
- Defining mechanisms controlling aberrant Fn14 regulation in cancer progression
- Exploring emerging roles of p53 isoforms in epigenetic dysregulation in cancer
- Investigation of a Wnt/cohesin cause for AML
- Investigation of the connection between cohesin's roles in cell division and gene expression in embryonic cell fate commitment