Specificity and disease in the Ubiquitin system
1:00pm - 2:00pm /
Monday 27th November 2017
/ Venue: Lecture Theatre 1 Life Sciences Building
- Kelly Welburn
- Suitable for: Suitable for staff and students at the University of Liverpool
- Admission: Free Event
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Helen Walden (University of Dundee)
Post-translational modification by ubiquitin is an essential regulatory process. My goal is to understand how ubiquitin is ligated to substrates. The Fanconi Anemia pathway is an exquisitely specific system, employing one E2 to target a single lysine on each of two homologous substrates. This signal is required for repair of DNA interstrand crosslinks. Conversely, the E3 ligase Parkin, mutated in hereditary Parkinsonism, has multiple substrates, targets multiple lysines, and collaborates with many E2s. Thus each system presents an intriguing set of questions regarding substrate specificity, chain type, and regulation. I will present an overview our efforts to address the questions of specificity and disease in the ubiquitin system.
Post-translational modification by ubiquitin is an essential regulatory process. My goal is to understand how ubiquitin is ligated to substrates. The Fanconi Anemia pathway is an exquisitely specific system, employing one E2 to target a single lysine on each of two homologous substrates. This signal is required for repair of DNA interstrand crosslinks. Conversely, the E3 ligase Parkin, mutated in hereditary Parkinsonism, has multiple substrates, targets multiple lysines, and collaborates with many E2s. Thus each system presents an intriguing set of questions regarding substrate specificity, chain type, and regulation. I will present an overview our efforts to address the questions of specificity and disease in the ubiquitin system.