Tsinghua’s Shi Yigong Awarded Aminoff Prize 2014

Beijing, April 8, 2014, — Professor Shi Yigong, Dean of School of Life Sciences, Tsinghua University, was awarded the Gregori Aminoff Prize in Crystallography 2014 at the Royal Swedish Academy of Sciences’ Annual Meeting on March 31. He is the first scientist from China who has won the Prize since it was established in 1979.
Prof. Shi Yigong (left) receives the Aminoff Prize.

Professor Shi was awarded the prize “for his groundbreaking crystallographic studies of proteins and protein complexes that regulate programmed cell death”, according to the Royal Swedish Academy of Sciences.

In order for an organism to survive, its cells need to be replaced regularly; for each cell that dies a new cell has to be created. Programmed cell death (apoptosis) is thus an important mechanism for all living organisms as the amount of cells in the organism needs to be constant. Each day billions of cells die due to apoptosis and equilibrium is maintained due to the same amount of cells being born. The process of apoptosis is very carefully regulated by a large amount of pro- and anti-apoptotic proteins that interplay in a very intricate and complex manner.

Shi’s crystallographic studies of the proteins that are part of the apoptotic machinery have not only resulted in the mapping of the proteins’ three-dimensional structures, but have also led to a detailed understanding of the mechanisms that regulate the system. Shi has studied apoptotic mechanisms in human cells, as well as in fruit flies (Drosophila melanogaster) and roundworms (Caenorhabditis elegans). Shi Yigong and his collaborators have mapped the complex structural foundation for the activation of pro-apoptotic caspase enzymes, i.e., the enzymes that activate cell death, and they have demonstrated the significance of a carefully regulated interplay between different proteins in the cell.

Prof. Shi has also contributed many pioneering insights to other scientific fields. His research team has, for instance, determined the structure of one variant of the presenilin family, a group of transmembrane enzymes that among other things play a part in the genesis and development of Alzheimer’s disease.