Postoctoral Research Assistant - MRC PPU - UOD1150
| Dyddiad hysbysebu: | 21 Mawrth 2024 |
|---|---|
| Cyflog: | £36,024 i £44,263 bob blwyddyn |
| Oriau: | Llawn Amser |
| Dyddiad cau: | 20 Ebrill 2024 |
| Lleoliad: | Dundee, Dundee, DD1 4HN |
| Cwmni: | University of Dundee |
| Math o swydd: | Dros dro |
| Cyfeirnod swydd: | 3281_1711014408 |
Crynodeb
Organelle-selective autophagy (OSA) is emerging as a critical and highly coordinated cellular process and its dysfunction is linked to cancer and neurological diseases. Crucially, OSA requires the timely ubiquitination of substrates, yet the E3 ligases involved and how their activity is regulated are poorly understood. Our lab has pioneered the development of activity-based probes for ~350 E3 ligases, and this project will deploy them on a proteome-scale to detect changes in E3 activity upon OSA (Pao et al., Nat Chem Biol 2016; Pao et al. Nature 2018; Mathur et al. Cell Chem Biol 2020). The role of E3 ligases in will be validated and their regulatory mechanism delineated. For informal enquiries please contact Prof. Satpal Virdee s.s.virdee@dundee.ac.uk.
Passionate candidates should ideally have recently carried out a PhD working in cell biology or biochemistry. The position will be a fantastic opportunity for candidates to broaden their skillset by working in a multidisciplinary lab using state-of-the-art technologies.
Your priorities include:
- Plan and carry out multidisciplinary research program aimed at identifying E3 ligases regulating organelle selective autophagy
- Presentation of research at lab meetings and scientific meetings
- Preparation of data for manuscript preparation
- Liaise with other lab members and collaborators
- Maintenance of meticulous lab records
Looking for:
Passionate candidates should ideally have recently carried out a PhD working in the biochemistry, structural biology or cell biology.
- A passion for ubiquitin biology
- Experience in cell biology or biochemistry
MRC Protein Phosphorylation and Ubiquitylation Unit (MRC PPU):
The MRC PPU is one of the world's most renowned centres for research on protein phosphorylation and ubiquitylation (http://www.ppu.mrc.ac.uk/). Many world-leading researchers in the field of signal transduction have trained within the
MRC PPU. The major aims of the MRC PPU are to advance understanding of the role of protein phosphorylation and ubiquitylation in cell regulation and human disease, to facilitate the development of drugs to treat diseases caused by abnormalities in phosphorylation, to generate reagents and improve technologies. A key remit of the MRC PPU is to train the next generation of scientists who will advance our understanding in this crucial area of medical research.
Division of Signal Transduction Unit (DSTT):
The Division of Signal Transduction Therapy (DSTT) was established in 1998. This division operates as a unique collaboration between scientists in the MRC PPU (Dario Alessi, Philip Cohen, Paul Davies, Virginia De Cesare, Greg Findlay, Ian Ganley, Yogesh Kulathu, Karim Labib, Amos Liang, Miratul Muqit, John Rouse, Adrien Rousseau, Gopal Sapkota, Esther Sammler, Mahima Swamy, Kirby Swatek, Satpal Virdee) and signalling researchers at the University of Dundee's School of Life Sciences (Simon Arthur, Doreen Cantrell, Alessio Ciulli, Ron Hay, Angus Lamond, Henry Mcsorley, Ignacio Moraga, Adrian Saurin,) and three leading pharmaceutical companies (Boehringer lngelheim, GlaxoSmithKline, Merck Serono). The DSTT is widely regarded as a model for how academia should interact with industry. The DSTT operates as a simple bridging mechanism to enable our Pis working on ubiquitylation and phosphorylation to effectively interact with three major pharmaceutical companies to help accelerate the early stages of drug discovery. The DSTT model enables industrial researchers working in any of the worldwide outlets of three pharmaceutical companies to effectively work with the ~200 Dundee-based researchers that participate in the collaboration to understand the fundamentals of the molecular causes of disease that result from disruptions in protein phosphorylation and ubiquitylation networks.