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Ping Wei


Ping Wei


Email: anddywei(at)gmail(dot)com;



Lab Homepage: http://cqb.pku.edu.cn/WeiLab


Research Area:

The ability to sense the environmental signal and make proper decisions is crucial for biology. A number of highly conserved signaling transduction kinase modules evolved to deal with environmental signals with complicated response dynamics. The spatial, temporal and quantitative changes of signaling dynamics determine cell-fate, such as proliferation, differentiation, and apoptosis. Despite the individual components of these kinase modules have been characterized, it is very challenging to fully understand the relationship of network topology and signal behavior due to the complexity of the kinase networks. The newly emerging discipline of Synthetic Biology enables a forward engineering approach to study cell signaling behavior in a quantitative and predictive manner by building man-made networks. We will use synthetic biology approach to study several evolutionally conserved kinase modules, such as the mitogen-activated protein kinase (MAPK) signaling cascade and the nuclear factor-kappa B (NF-B) signaling pathway. We want to understand 1) what specific signal dynamics these kinase modules are capable of, 2) how their signal processing capabilities are important for physiological functions, 3) can I reprogram them to change the signaling behaviors for novel functions, 4) are there any general principles for designing biological networks.


Selected Publications:

1. Mitchell, A., Wei, P.*, Lim, A.W.*, Oscillatory stress stimulation uncovers an Achilles’ heel of the yeast MAPK signaling network. Science 2015; 350, 1379-1383. (*co-corr. author)

2. Martin, H., Shales, M., Fernandez-Pinar, P., Wei, P., Molina, M., Fiedler, D., Shokat, K. M., Beltrao, P., Lim, W., Krogan, N. J. Differential genetic interactions of yeast stress response MAPK pathways. Molecular Systems Biology 2015; 11, 800.

3. Wei, P.*, Wong, W.W.*, Park, J.S., Corcoran, E. E., Peisajovich, S. G., Onuffer, J, J., Weiss, A., Lim, W.A. Bacterial virulence proteins as tools to rewire kinase pathways in yeast and immune cells. Nature 2012; 488, 384-388.

4. Peisajovich, S.G., Garbarino, J.E., Wei, P., Lim, W.A. Rapid diversification of cell signaling phenotypes by modular domain recombination. Science 2010; 328, 368-372

5. Liang H., Chen, H., Fan, F., Wei, P., Guo, X., Jin, C., Zeng, C., Tang, C., Lai, L. De novo design of a beta alpha beta motif. Angew Chem Int Ed Engl. 2009; 48(18):3301-3.

6. Chen, H.*, Wei, P.*, Huang, C., Tan, L., Liu, Y., Lai, L. Only one protomer is active in the dimer of SARS 3C-like proteinase. J. Biol. Chem. 2006; 281: 13894-13898.

7. Wei, P.*, Fan, K.*, Chen, H., Ma, L., Huang, C., Tan, L., Xi, D., Li, C., Liu, Y., Cao, A., Lai, L. The N-terminal octapeptide acts as a dimerization inhibitor of SARS coronavirus 3C-like proteinase. Biochem. Biophys. Res. Commun. 2006; 339: 865-872.

8. Fan, K.*, Wei, P.*, Feng, Q., Chen, S., Huang, C., Ma, L., Lai, B., Pei, J., Liu, Y., Chen, J., Lai, L. Biosynthesis, purification, and substrate specificity of severe acute respiratory syndrome coronavirus 3C-like proteinase. J. Biol. Chem. 2004; 279: 1637-1642.

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