Professional Education

  • Doctor of Philosophy, Tsinghua University (2013)
  • Bachelor of Science, Sichuan University (2008)

Stanford Advisors


All Publications

  • Structural insights into mu-opioid receptor activation NATURE Huang, W., Manglik, A., Venkatakrishnan, A. J., Laeremans, T., Feinberg, E. N., Sanborn, A. L., Kato, H. E., Livingston, K. E., Thorsen, T. S., Kling, R. C., Granier, S., Gmeiner, P., Husbands, S. M., Traynor, J. R., Weis, W. I., Steyaert, J., Dror, R. O., Kobilka, B. K. 2015; 524 (7565): 315-?
  • Propagation of conformational changes during mu-opioid receptor activation NATURE Sounier, R., Mas, C., Steyaert, J., Laeremans, T., Manglik, A., Huang, W., Kobilka, B. K., Demene, H., Granier, S. 2015; 524 (7565): 375-?
  • Mechanistic insights into CED-4-mediated activation of CED-3 GENES & DEVELOPMENT Huang, W., Jiang, T., Choi, W., Qi, S., Pang, Y., Hu, Q., Xu, Y., Gong, X., Jeffrey, P. D., Wang, J., Shi, Y. 2013; 27 (18): 2039-2048


    Programmed cell death in Caenorhabditis elegans requires activation of the caspase CED-3, which strictly depends on CED-4. CED-4 forms an octameric apoptosome, which binds the CED-3 zymogen and facilitates its autocatalytic maturation. Despite recent advances, major questions remain unanswered. Importantly, how CED-4 recognizes CED-3 and how such binding facilitates CED-3 activation remain completely unknown. Here we demonstrate that the L2' loop of CED-3 directly binds CED-4 and plays a major role in the formation of an active CED-4-CED-3 holoenzyme. The crystal structure of the CED-4 apoptosome bound to the L2' loop fragment of CED-3, determined at 3.2 Å resolution, reveals specific interactions between a stretch of five hydrophobic amino acids from CED-3 and a shallow surface pocket within the hutch of the funnel-shaped CED-4 apoptosome. Structure-guided biochemical analysis confirms the functional importance of the observed CED-4-CED-3 interface. Structural analysis together with published evidence strongly suggest a working model in which two molecules of CED-3 zymogen, through specific recognition, are forced into the hutch of the CED-4 apoptosome, consequently undergoing dimerization and autocatalytic maturation. The mechanism of CED-3 activation represents a major revision of the prevailing model for initiator caspase activation.

    View details for DOI 10.1101/gad.224428.113

    View details for Web of Science ID 000324872100008

    View details for PubMedID 24065769

  • A proposed role for glutamine in cancer cell growth through acid resistance CELL RESEARCH Huang, W., Choi, W., Chen, Y., Zhang, Q., Deng, H., He, W., Shi, Y. 2013; 23 (5): 724-727

    View details for DOI 10.1038/cr.2013.15

    View details for Web of Science ID 000318483200016

    View details for PubMedID 23357849

  • Crystal structure and biochemical analyses reveal Beclin 1 as a novel membrane binding protein CELL RESEARCH Huang, W., Choi, W., Hu, W., Mi, N., Guo, Q., Ma, M., Liu, M., Tian, Y., Lu, P., Wang, F., Deng, H., Liu, L., Gao, N., Yu, L., Shi, Y. 2012; 22 (3): 473-489


    The Beclin 1 gene is a haplo-insufficient tumor suppressor and plays an essential role in autophagy. However, the molecular mechanism by which Beclin 1 functions remains largely unknown. Here we report the crystal structure of the evolutionarily conserved domain (ECD) of Beclin 1 at 1.6 Å resolution. Beclin 1 ECD exhibits a previously unreported fold, with three structural repeats arranged symmetrically around a central axis. Beclin 1 ECD defines a novel class of membrane-binding domain, with a strong preference for lipid membrane enriched with cardiolipin. The tip of a surface loop in Beclin 1 ECD, comprising three aromatic amino acids, acts as a hydrophobic finger to associate with lipid membrane, consequently resulting in the deformation of membrane and liposomes. Mutation of these aromatic residues rendered Beclin 1 unable to stably associate with lipid membrane in vitro and unable to fully rescue autophagy in Beclin 1-knockdown cells in vivo. These observations form an important framework for deciphering the biological functions of Beclin 1.

    View details for DOI 10.1038/cr.2012.24

    View details for Web of Science ID 000300942400006

    View details for PubMedID 22310240

  • Structure of the formate transporter FocA reveals a pentameric aquaporin-like channel NATURE Wang, Y., Huang, Y., Wang, J., Cheng, C., Huang, W., Lu, P., Xu, Y., Wang, P., Yan, N., Shi, Y. 2009; 462 (7272): 467-U158


    FocA is a representative member of the formate-nitrite transporter family, which transports short-chain acids in bacteria, archaea, fungi, algae and parasites. The structure and transport mechanism of the formate-nitrite transporter family remain unknown. Here we report the crystal structure of Escherichia coli FocA at 2.25 A resolution. FocA forms a symmetric pentamer, with each protomer consisting of six transmembrane segments. Despite a lack of sequence homology, the overall structure of the FocA protomer closely resembles that of aquaporin and strongly argues that FocA is a channel, rather than a transporter. Structural analysis identifies potentially important channel residues, defines the channel path and reveals two constriction sites. Unlike aquaporin, FocA is impermeable to water but allows the passage of formate. A structural and biochemical investigation provides mechanistic insights into the channel activity of FocA.

    View details for DOI 10.1038/nature08610

    View details for Web of Science ID 000272144200035

    View details for PubMedID 19940917