报告题目：Chemoproteomic approaches towards mapping cysteine modifications
报告人：杨靖博士(Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN, US)
报告时间：2014年12月30日（星期二）上午9:00
报告地点：独墅湖校区二期云轩楼2301室
报告摘要：
The nucleophilic thiol group allows cysteines to undergo a broad range of chemical modifications, including redox reactions, alkylation, and metal binding, which are important for protein structure, localization, regulation. However, methodological limits have so far prevented a proteome-wide analysis of the substrates and specific sites of these modifications. We apply chemical probes and mass spectrometry-based chemoproteomics to investigate protein targets of oxidation-related thiol modifications, including total cysteine oxidation, S-sulfenylation and S-alkylation by lipid-electrophile in complex proteomes. Using this strategy, we are able to (1) quantify changes of over 5000 reactive cysteine residues in proteomes in response to exogenous hydrogen peroxide stimulation, (2) site-specifically map and quantify over 1000 unstable S-sulfenylation events in cells, and (3) directly identify and quantify ~400 S-alkylations by lipid-derived electrophiles in cells. These studies not only greatly expand the catalogue of thiol proteins that undergo these modifications in cells, but also suggest novel redox mechanisms that contribute to key biological functions of several proteins. For example, SIRT6, a member of a conserved family of NAD+-dependent deacetylases, may exert redox control of HIF1A transcriptional activity through reversible formation of disulfide-linked SIRT6-HIF1A complex. Taken together, these studies provide a new view of the landscape of thiol modifications in proteomes and suggests new hypotheses for future exploration of redox signaling and oxidative stress.
报告人简介：
Jing Yang, Ph.D. was born in 1985 in Changsha, Hunan. He received his BSc (2007) and Ph.D. degree (2012) from China Pharmaceutical University under guidance of professor Li Ding. Afterwards, He worked as a postdoctoral research fellow with professor Daniel C. Liebler at the Vanderbilt University. His current work is mainly focused on cysteine modification and its role in redox regulation of protein functions. He received the ACS Award for Young Investigator in 2013.
