Unpicking the Specificity of the Protein Quality Control Network in Health and Disease

Year of award: 2021


  • Dr Theodoros Karamanos

    University of Leeds, United Kingdom

Project summary

Protein molecules perform most of the necessary functions to keep cells alive. To do so, they often must adopt a highly specific shape (or fold). However, key proteins sometimes misfold, causing diseases such as Alzheimer's and diabetes, leading to more than 120,000 deaths every year. Fortunately, ours cells have developed a sophisticated network to protect against misfolding which involves a dedicated set of guardian proteins, called chaperones. Chaperones cooperate with each other in order to bind misfolded protein molecules, thereby preventing cell death and minimising the effects of ageing. It is important to understand how chaperones are so effective in recognising malicious protein states so we can design better therapeutic strategies against these devastating diseases. Using the DNAJB6 chaperone, that is implicated in neurodegeneration, myopathies and cancer, I will uncover the mechanisms that govern the functions of the chaperone network and how it can defeat specific threats against cell integrity.