Department of Medicine

Department of Medicine

  Division of Pulmonary, Allergy and Critical Care Medicine

Faculty Profile: JING ZHAO, MD, PhD


Dr. Jing Zhao's Research

1). The ubiquitin-proteasome system is the major pathway of non-lysosomal intracellular protein degradation. The ubiquitin system consists of the concerted actions of three enzyme complex (E1, E2, E3) that link ubiquitin chains onto target proteins to mark them for degradation. This tagging process leads to their recognition by the 26S proteasome, a very large multicatalytic protease complex. The protein unbiquitination is a reversible process and controlled by deubiquitinating enzymes (DUBs). The ubiquitin-proteasome system controls pro- and anti-inflammatory responses by modulating immune regulatory signal protein turnover.  Currently her research focuses on the molecular regulation of immune regulatory protein stability such as Creb-binding protein CBP.

2). Dr. Zhao is also interested in proteomic studies of proteins that play critical roles in acute lung injury. Cell membrane rafts are dynamic assemblies of proteins and lipids within the plasma membrane which are enriched in sphingolipids and cholesterol and have been implicated in dynamic membrane signaling and trafficking.  In response to diverse extracellular stimuli, a variety of proteins are selectively enriched in cell membrane rafts, including G-protein-coupled receptors (GPCR), proteins involved in cell signaling, non-receptor tyrosine kinases (i.e. Src family kinases) and their downstream targets. She is interested in the areas of protein identification and characterization, and quantitative proteomic analysis of plasma membrane proteins in lipid raft which are involved in cell signaling and trafficking.  In particular she has studied sphingosine-1-phosphate (S1P) induced lipid rafts by usingquantitative proteomic approaches.

3). Post-translational modifications have critical roles in all the major cellular pathways and diseases. Protein phosphorylation is a critical and common type of post-translational protein modification that reflects the dynamic activities of both protein kinases and protein phosphatases. The reversibility of protein phosphorylation affords it versatile functions for cell regulation such as cell division, differentiation, proliferation, and signaling transduction. Her interest is the development and application of proteomic technologies and bioinformatics tools for characterizing modifications of key proteins in acute lung injury.  She currently focuses on protein ubiquititation and phosphorylation modification.