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Dr. Feng Shao’s Lab
Feng Shao,Ph.D
Associate Investigator, NIBS, Beijing, China
Phone： 86-10-80726688-8560
Fax： 86-10-80728046
Room Number：B344
E-mail: shaofeng@nibs.ac.cn |
Research Description:
Dr. Feng Shao’s laboratory is interested in studying the process of bacterial pathogen-host interaction at the molecular level. The goal of this research direction is to reveal novel mechanisms utilized by bacterial pathogen to thwart host immune signaling transduction pathway. Dr. Feng Shao’s lab has recently discovered a novel family of enzymes termed phosphothreonine lyase from a wide array of bacterial pathogens including Shigella and Salmonella.  These bacterial proteins can irreversibly “dephosphorylate” the host MAP Kinases through a beta elimination reaction, which results into the permanent inactivation of these kinases and downregulation of the host innate immune signal transduction pathway. Combining various biochemical and genetic approaches, the lab is currently investigating the function of several other pathogenic effectors from Shigella flexneri and how these effectors work together to interfere the host immune signal transduction pathway.  Dr. Feng Shao is also interested in the role of CUL3-mediate ubiquitination and degradation pathway in cell cycle regulation, cell growth and tumorigenesis. His research has demonstrated that BTB domain-containing proteins serve as substrate-specific adaptors for the CUL3 ubiquitin ligase complex, a novel, SCF-like ubiquitin ligase complex with little understanding. He has isolated several novel BTB domain proteins with potential function in normal and tumor cell proliferation, and his group is currently investigating the mechanism of these novel protein ubiquitination and degradation pathway in regulating cell proliferation.
Publications:
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1. |
Ge J, Xu H, Li T, Zhou Y, Zhang Z, Li S, Liu L, Shao F. (2009) A Legionella type IV effector activates the NF-κB pathway by phosphorylating the IκB family of inhibitors. Proc. Natl. Acad. Sci., 106, 13725-13730 |
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Chen Y, Yang Z, Meng M, Zhao Y, Dong N, Yan H, Liu L, Ding M, Peng, HB, Shao F. (2009) Cullin Mediates Degradation of RhoA through Evolutionarily Conserved BTB Adaptors to Control Actin Cytoskeleton Structure and Cell Movement. Mol. Cell, 35, 841-855 |
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3. |
Dowen RH, Engel JL, Shao F, Ecker JR, Dixon JE. (2009) A Family of Bacterial Cysteine Protease Type III Effectors Utilizes Acylation-dependent and -independent Strategies to Localize to Plasma Membranes. J. Biol. Chem., 284, 15867-15879 |
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Yao Q, Cui J, Zhu Y, Wang G, Hu L, Long C, Cao, R, Liu X, Huang N, Chen S, Liu L, Shao F. (2009) A bacterial type III effector family uses the papain-like hydrolytic activity to arrest the host cell cycle. Proc. Natl. Acad. Sci., 106, 3716-3721 |
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5. |
Zhu Y., Li H., Hu L., Wang, J., Zhou Y., Pang Z., Liu L., Shao F. (2008) Structure of a Shigella effector reveals a new class of ubiquitin ligases. Nature Structural & Molecular Biology, 15, 1302-8 |
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Shao F. (2008) Biochemical functions of Yersinia type III effectors. Current Opinion in Microbiology, 11, 21-29 (invited review) |
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Zhu Y, Li H, Long C, Hu L, Xu H, Liu L, Chen S, Wang DC, Shao F. (2007) Structural insights into the enzymatic mechanism of the pathogenic MAPK phosphothreonine lyase. Mol. Cell, 28, 899-913 |
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Zhang J, Shao F, Li Y, Cui H, Chen L, Li H, Zou Y, Long C , Lan L, Chai J, Chen S, Tang X, Zhou JM. (2007) A Pseudomonas syringae effector inactivates MAPKs to suppress PAMP-induced immunity. Cell Host & Microbe, 1, 175-185. |
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9. |
Li H, Xu H, Zhou Y, Zhang J, Long C, Li S, Chen S, Zhou JM, Shao F. (2007) The phosphothreonine lyase activity of a bacterial type III effector family. Science, 315, 1000-1003. |
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10. |
Alto NM, Shao F, Lazar CS, Brost RL, Chua G, Mattoo, SM, McMahon SA, Ghosh P, Hughes TR, Boone C, Dixon JE. (2006) Identification of a bacterial type III effector family with G-protein mimicry functions. Cell, 124, 133-145. |
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Zhu M, Shao F, Innes RW, Dixon JE, Xu Z. (2004) The crystal structure of Pseudomonas avirulence protein AvrPphB: a papain-like fold with a distinct substrate-binding site. Proc. Natl. Acad. Sci., 101, 302-307 |
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12. |
Shao F, Golstein, C, Ade J, Stoutemyer M., Dixon JE, Innes RW. (2003) Cleavage of Arabidopsis PBS1 by a bacterial type III effector. Science, 301, 1230-1233. |
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13. |
Shao F, Vacratsis PO, Bao Z, Bowers KE, Fierke CA, Dixon JE. (2003) Biochemical characterization of the Yersinia YopT protease: cleavage site and recognition elements in Rho GTPases. Proc. Natl. Acad. Sci., 100, 904-909. |
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Shao F, Merritt PM, Bao Z, Innes RW, Dixon JE. (2002) A Yersinia effector and a Pseudomonas avirulence protein define a family of cysteine proteases functioning in bacterial pathogenesis. Cell, 109, 575-588. |
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15. |
Juris SJ, Shao F, Dixon JE. (2002) Yersinia effectors target mammalian signaling pathways. Cell. Microbiol., 4: 201-11. (Co-first author) |
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16. |
Bian X, McAllister-Lucas LM, Shao F, Schumacher KR, Feng Z, Porter AG, Castle VP, Opipari AW, Jr. (2001) NF-kappa B activation mediates doxorubicin-induced cell death in N-type neuroblastoma cells. J. Biol. Chem., 276, 48921-9. |
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17. |
Shao F, Bader MW, Jakob U, Bardwell JC. (2000) DsbG, a protein disulfide isomerase with chaperone activity. J. Biol. Chem., 275, 13349-52. |
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18. |
Wang CG, He XL, Shao F, Liu W, Ling MH, Wang DC, Chi CW. (2001) Molecular characterization of an anti-epilepsy peptide from the scorpion Buthus martensi Karsch. Eur. J. Biochem., 268, 2480-5. |
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Shao F, Hu Z, Xiong YM, Huang QZ, Wang CG, Zhu RH, Wang DC. (1999) A new antifungal peptide from the seeds of Phytolacca americana: characterization, amino acid sequence and cDNA cloning. Biochim. Biophys. Acta, 1430, 262-8. |
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20. |
Shao F, Xiong YM, Zhu RH, Ling M, Chi CW, Wang DC. (1999) Expression and purification of the BmK M1 neurotoxin from the scorpion Buthus martensii Karsch. Protein Expr. Purif., 17, 358-65. |
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