Dr Chun Guo
Room: B2 221a Alfred Denny building
Brief career history
My research interests are to understand the basic cell biology and signaling pathways associated with protein post-translational modifications (PTMs, e.g., Proteolytic Cleavage, Phosphorylation, Ubiquitination and SUMOylation) in cell death, survival and repair following stress, and to translate the findings into animal models of human diseases and into treatments for human disease.
Protein SUMOylation and deSUMOylation in health and disease.
One type of PTM is SUMOylation, which involves the attachment of a small protein called Small Ubiquitin-related Modifier (SUMO) to target proteins. SUMOylation is essential for the survival of all plant and animal cells because it regulates protein-protein interactions, either promoting or hindering specific interactions according to the molecular environment.
Thus the functional consequences of SUMO attachment vary greatly depending on the substrate and the cell type, and in most cases remain only poorly understood. SUMOylation can be reversed by the action of SUMO proteases to cleave the bond between proteins. This is called deSUMOylation. The largest and most characterised family of SUMO proteases is that of the sentrin-specific proteases (SENPs). Specific targets and physiological roles for SENPs are largely unknown.
In my laboratory a combination of techniques including molecular cell biology, biochemistry, genetics, pharmacology and histology is used to address the roles of protein SUMOylation and deSUMOylation in health and disease, particularly in neurodegenerative disorders such as dementia and amyotrophic lateral sclerosis (ALS).
The results may lead to better understanding of disease processes, more effective therapies, an enhancement to the quality of life of both patients and their carers and finally, an easing of the substantial economic burden which dementia and ALS currently impose.
Undergraduate and postgraduate taught modules
Level 1 modules:
Level 2 modules:
Level 3 modules:
- Increased SUMO-2/3-ylation mediated by SENP3 degradation is protective against cadmium-induced caspase 3–dependent cytotoxicity. Journal of Toxicological Sciences, 42(5), 529-538. View this article in WRRO
- SENP3-mediated deSUMOylation of Drp1 facilitates interaction with Mff to promote cell death.. Scientific Reports, 7. View this article in WRRO
- Wrestling with stress: Roles of protein SUMOylation and deSUMOylation in cell stress response. IUBMB Life, 66(2), 71-77.
- The β-Arrestin-2 Scaffold Protein Promotes c-Jun N-terminal Kinase-3 Activation by Binding to Its Nonconserved N Terminus. Journal of Biological Chemistry, 283(23), 15903-15911.
- Absence of α7 integrin in dystrophin-deficient mice causes a myopathy similar to Duchenne muscular dystrophy. Human Molecular Genetics, 15(6), 989-998.
- Paradigmatic identification of MMP-2 and MT1-MMP activation systems in cardiac fibroblasts cultured as a monolayer. Journal of Cellular Biochemistry, 94(3), 446-459.
- Type I Collagen-induced MMP-2 Activation Coincides with Up-regulation of Membrane Type 1-Matrix Metalloproteinase and TIMP-2 in Cardiac Fibroblasts. Journal of Biological Chemistry, 278(47), 46699-46708.
- SENP3-mediated deSUMOylation of dynamin-related protein 1 promotes cell death following ischaemia. The EMBO Journal, 32(11), 1514-1528. View this article in WRRO