News from DCEXS-UPF
A new article by the Oxidative Stress and Cell Cycle research group at the Department of Experimental and Health Sciences, Pompeu Fabra University (DCEXS-UPF) identifies the main strategy of cells to deal with the accumulation of misfolded proteins. In the paper, published in the journal Cell Reports, the Schizosaccharomyces pombe yeast model has been used to investigate the protein quality control process.
Proteins are made up of chains of amino acids and during their formation they must fold to acquire an appropriate shape enabling them to perform their functions. However, when cells are subjected to stress or harm, such as high temperatures, some of the proteins may not fold properly. In this study, the researchers posed the question: what do cells do with misfolded proteins?
There are three ways to solve the problem. The first option is to try to fix the folding in order to regain function, but this can be tricky because if stress conditions continue, the proteins continue unfolding. A second way is to destroy proteins that have not properly folded by way of a machinery called proteasome. “But, in this study we reveal that the dominant route in yeast is a third option consisting of the formation of aggregates to protect misfolded proteins from degradation”, Elena Hidalgo, researcher of the study, explains.
Cabrera, M., Boronat, S., Marte, L., Vega, M., Pérez, P., Ayté, J. and Hidalgo, E. February, 2020. Chaperone-facilitated aggregation of thermo-sensitive proteins shields them from degradation during heat stress. Cell Rep. DOI: 10.1016/j.celrep.2020.01.077.