PSC Frontier Seminar series
Title: Mapping the Cysteine Redoxome
Speaker: Prof. Jing Yang, State Key Laboratory of Proteomics, National Center for Protein Sciences • Beijing, Beijing Proteome Research Center, Institute of Lifeomics, Beijing 102206, China
Time: 15:00 pm
Day/Date: Apr. 30th, 2019 (Tuesday)
Host: Prof. Pengcheng Wang
Venue: No.1 meeting room
The sulfur atom of cysteine can assume many different redox states, which exhibit distinct chemical properties. Like phosphorylation and dephosphorylation, redox changes on cysteine residues can reversibly alter protein function, representing a crucial mechanism in cellular regulation and signaling. However, efforts to understand their functional roles in biology and disease have been hampered due to limitations of methods for globally analyzing site-specific protein targets and redox dynamics. In the past five years, we develop several site-centric quantitative chemoproteomic approaches to systematically quantify cysteine reactivities and to globally map and quantify distinct types of cysteine modifications, such as S-sulfenylation (Cys-SOH), S-sulfinylation (Cys-SO2H), and S-persulfidation (Cys-SSH), in complex proteomes. We have applied these chemoproteomic tools to various human cells and model organisms, including M. musculus, D. melanogaster, and A. thaliana, providing the largest cysteine redoxome dataset. The dataset will be freely accessible as a web portal resource at OXID (http://redox.ncpsb.org/OXID/). Notably, these analyses also reveal novel redox mechanisms of several proteins with key biological functions, including S-sulfenyl-mediated redox relay, and greatly expand the substrate spectrum of many functionally important reductases, including thioredoxin and sulfiredoxin. Taken together, our chemoproteomic toolbox provides a great opportunity to study cysteine-mediated redox networks in a range of biological processes and adaptive responses in physiology and pathophysiology.
The seminar will be delivered in English.