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Home > Academics > Biology > Faculty > Rao Feng


Rao Feng

Associate Professor

Department of Biology


Research Interests:

Cell Signaling via small messenger molecules. The main interest of our group is to elucidate the function and mechanism of small molecules that are emerging messengers. Inositol triphosphates (IP3) is a well-established 2nd messenger transducing extracellular stimulus into intracellular activities. IP3 is step-wise phosphorylated by a family of inositol phosphate kinases generating higher inositol polyphosphates (IP4-8) whose physiology remains poorly understood. In particular, inositol pyrophosphates (IP7/8) containing energetic pyrophosphate bond(s) are enigmatic inositol derivatives dynamically generated from inositol hexakisphosphate (IP6) by IP6 kinases (IP6Ks) and IP7 kinases (PPIP5Ks). By studying the regulation of IP6Ks and enzymes leading to IP6 production in cell- and animal-based models, we aim to uncover the (patho)physiology (e.g. cell migration and cancer metastasis) and signal transduction pathways mediated by inositol pyrophosphates. On top of this, we employ chemical and biochemical approaches to identify effector modules and their mode of interactions, with the goal to unravel underlying principles of inositol pyrophosphate signaling. Given the key roles of IP6K/IP7 in tumor progression and other diseases processes, the mechanistic and functional insights gained from this investigation will hopefully provide new therapeutic targets.


Professional Experience:
2016 - Present        Associate Professor, Department of Biology, SUSTech
2015-2016              Assistant Investigator, National Institute of Biological Sciences, Beijing, China
2011-2015              Postdoctoral Fellow, Johns Hopkins University School of Medicine, Maryland, USA
2006-2007              Project Officer, School of Biological Sciences, Nanyang Technological University, Singapore
2005-2006              Research Assistant, Department of Biological Sciences, National University of Singapore, Singapore


Educational Background:
2007-2011      Ph. D., School of Biological Sciences, Nanyang Technological University, Singapore
2001-2005      B.Sc., Biomedical Sciences, National University of Singapore, Singapore



Open Positions:
◆ We are currently recruiting motivated lab members including students and employee at all levels. 
To apply, please send your CV to



Selected Publication:
Research publications
1.    Scherer, PC. #, Ding, Y. #, Liu, Z., Xu, J., Haibin, Moa., Barrow, JC., Ning, W., Zheng, N., Snyder, SH. *, Rao F*. Inositol hexakisphosphate (IP6) generated by IP5K mediates cullin-COP9 signalosome interactions and CRL function. Proc. Natl. Acad. Sci. 2016 113, 3503-8 (# = Co-first author; * = Corresponding author).
2.    Rao F.#, Xu, J.#, Fu, C., Cha, J., Xu, R., Gadalla, MM., Wu, M., Fiedler, D., Barrow, JC., Snyder, SH. Inositol pyrophosphates promote cancer growth and metastasis by antagonizing the tumor suppressor LKB1. Proc. Natl. Acad. Sci. 2015 112, 1773-8.
3.    Rao F.#, Xu, J.#, Kahn, AB., Cha, J., Xu, R. Tyagi, R., Dang, Y., Chakraborty, A., Snyder, SH. Inositol hexakisphosphate kinase-1 mediates assembly/ disassembly of the CRL4-Signalosome complex to regulate DNA repair and cell death. Proc. Natl. Acad. Sci. 2014 111, 16005-16010.
4.    Rao F., Cha, J., Xu, J., Xu, R., Vandiver, MS., Tokhunt, RT., Wu, M., Fiedler, D., Barrow, J., Snyder, SH. Inositol pyrophosphates mediate the DNA-PK/ATM-p53 cell death pathway by regulating CK2 phosphorylation of Tti1/Tel2. Mol. Cell 2014 54, 119-32.
5.    Rao, F., See, RY., Zhang, D., Toh, DC., Liang Z-X. YybT is a signaling protein that contains a cyclic-di-nucleotide phosphodiesterase domain and a GGDEF domain with ATPase activity. J. Biol. Chem. 2010, 285:473-82.
6.    Tan E.#, Rao F.#, Pasunooti S., Pham TH., Soehano I., Turner MS., Liew CW., Lescar J., Pervushin K., Liang Z-X. Solution structure of the PAS domain of a thermophilic YybT homolog reveals a potential ligand-binding site. J. Biol. Chem. 2013, 288:11949-59.
7.    Rao, F.*, Qi, Y., Murugan, E., Pasunooti, S., Ji, Q. 2',3'-cAMP hydrolysis by metal-dependent phosphodiesterases containing DHH, EAL, and HD domains is non-specific: implications for PDE screening. Biochem. Biophys. Res. Commun. 2010, 398:500-505. (*= Corresponding author).
8.    Rao, F., Pasunooti, S., Ng, Y., Zhuo, W., Lim, L., Liu, AW., Liang Z-X. Enzymatic synthesis of c-di-GMP using a thermophilic diguanylate cyclase. Anal. Biochem. 2009, 389:138-42.
9.    Rao, F., Ji, Q., Soehano, I., Liang, Z-X. Unusual Heme-Binding PAS Domain from YybT Family Proteins. J. Bacteriol. 2011, 193:1543-1551.
10.    Rao, F., Qi, Y., Chong, HS., Kotaka, M., Li, B., Lescar, J., Tang, K., Liang, Z-X. The functional role of a conserved loop in EAL domain-based c-di-GMP specific phosphodiesterase. J. Bacteriol. 2009, 191:4722-31.
11.    Rao, F., Yang, Y., Qi, Y., Liang, Z-X. Catalytic mechanism of C-di-GMP specific phosphodiesterase: a study of the EAL domain containing protein RocR from Psudomonas aeruginosa. J. Bacteriol. 2008, 190:3622-31.
12.    Rao, F., et al. Hong, Y. Medaka tert produces multiple variants with differential expression during differentiation in vitro and in vivo. Int. J. Biol .Sci. 2011, 7(4):426-439.

1.    Liang, Z-X., Rao, F. Diguanylate cyclase method of producing the same and its use in the manufacture of cyclic-di-GMP and analogues thereof. 2014, US Patent No: 8,859,237.

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