Research

Research

Research

WANG Tao

Life is the Miracle of Universe.

WANG Tao

汪涛

Institute of Infectious Diseases

Junior Principal Investigator


taowang@szbl.ac.cn

Timeline

  • 2019 - Present

    Shenzhen Bay Laboratory         Junior Principal Investigator & Ph.D Advisor

  • 2014 - 2019

    Southern University of Science and Technology         PI & Ph.D Advisor

  • 2011 - 2014

    Peking University         PI & Tenure-track Associate Professor & Ph.D Advisor

  • 2006 - 2011

    Brookhaven National Laboratory         Postdoc/Research Scientist

  • 2006

    Institute of Biophysics, Chinese Academy of Sciences         Research Assistant

  • 2001 - 2006

    Institute of Biophysics, Chinese Academy of Sciences         Ph.D.

  • 1997 - 2001

    Jilin University         B.S.











Research Areas


We try to understand the molecular mechanisms of key biomacromolecules in certain life processes, as well as the protein structures, functions and dynamics. X-ray Crystallography, Cryo-Electron Microscopy, molecular cloning, protein purification and biochemical studies are key parts of our research work.

 

We focus on the scientific questions of how signal transduces across cell membrane, and how viruses recognize the host cell for entry, then self-replicated and assembled for the new life cycle.











Highlights


1. Ligand-bound biological assembly of full-length human IGF-1 receptor. (Structure, 2020).

2. The molecular basis of IP6-dependent Cullin-RING E3 ubiquin ligase regulation by COP9-signalosome. (PNAS, 2020).

3. The key replication initiation factor Sap1 for the assembly of pre-Replication complex in Schizosaccharomyces pombe. (J Biol Chem, 2017).

4. The structural basis of the auto-inhibition of PLK1.(NSMB, 2010).

The binding-induced folding mechanism of prokaryotic ubiquitin like protein in the Pup-20S proteasome pathway in Mycobacterium tuberculosis. (Mol Microbiol, 2017; NSMB, 2010).


image.png

Prokaryotic-ubiquitin like protein (Pup) in Mycobacterium tuberculosis, like ubiquitin in eukaryotes, play its biological role as a tag, covalently linked to the doomed protein then deliver them to 20S proteasome for degradation. Pup adopts binding-induced folding mechanism on the mycobacterium proteasomal ATPase (Mpa), and hexametric Mpa has a b-grasp domain hinders direct docking with 20S proteasome and the Pup-20S proteasome pathway under precisely controlled. (Mol Microbiol, 2017; NSMB, 2010).




image.png

Tyrosine kinase receptor of insulin-like growth factor 1 receptor (IGF-1R) and insulin receptor (IR) bind to hormones, then transduces the signals across the cell membrane. We reconstructed the cryo-EM structures of human IGF-1R in complex with insulin or IGF-1, revealing the unique architecture of full-length human IGF-1R in active state. (Structure, 2020) 









Honors


1. 2016, Council member, Chinese Society of Molecular Biophysics

2. 2016, Outstanding young teachers in Colleges and Universities in Guangdong Province

3. 2016, Outstanding innovative young scientist in Guangdong Province

4. 2013, Chief scientist, The major scientific research program of the Ministry of science and technology, China

5. 2013, Overseas excellent talents, Shenzhen Municipal Government

6. 2012, Excellent Young Talents, Peking University

7. 2010: Spotlight Award, in recognition of exceptional job performance, Brookhaven

8. National Laboratory, USA.

9. 2010: Top5 scientific discoveries in 2010, Brookhaven National Laboratory, USA












Related News


1. 2020.08.25 Phoenix Satellite TV | Shenzhen Special Economic Zone: vigorously attracting talents and activating basic scientific research for 40 years.

    https://www.szbl.ac.cn/infomation/topic/mediareports/860.html 


2. 2020.04.15 The research progress of human IGF-1R and ubiquitin modification.

    https://www.szbl.ac.cn/infomation/research/813.html 


3. 2020.03.11 SZBL People |  Anti new coronavirus drugs may appear in these key processes.

    https://www.szbl.ac.cn/infomation/topic/interview/804.html 












Selected Publications


1. Zhang X, Yu DQ, Sun JC, Li XM, Liu L, Liu S, Liu JB, Wu YL, Li DY, Ma YP, Han X, Zhu YN, Wu ZL, Wang YH, Ouyang Q, Wang T*. Visualization of ligand-bound ectodomain assembly in the full-length human IGF-1 receptor by Cryo-EM single particle analysis. Structure. 2020 May 5;28,555-561. (*: Correspondence).

2. Lin H, Zhang XZ, Liu L, Fu QY, Zang CL, Ding Y, Xu ZX, He SN, Yang XL, Wei XY, Mao HB, Cui YS, Yi W, Zhou CZ, Du LL, Huang N, Zheng N, Wang T*, Rao F*. Molecular basis of IP6-dependent Cullin-RING ligase regulation by the COP9 Signalosome. Proc Natl Acad Sci U S A. 2020 Feb 25;117(8):4117-4124. (: Contributed equally) (*: Correspondence).

3. Xie MS, Zhao H, Liu QS, Zhu YJ, Yin F, Liang YJ, Jiang YH, Wang DY, Hu K, Qin X, Wang ZC, Wu YJ, Xu NH, Ye XY*, Wang T*, Li ZG*. Structural basis of inhibition of ERα-coactivator interaction by high-affinity N-terminus isoaspartic acid tethered helical peptides. J Med Chem. 2017 Nov 9;60(21):8731-8740. (*: Correspondence).

4. Wu YJ, Hu K, Yang SQ, Li DF, Bai L, Jastrab J, Gao Y, Hu YL, Darwin H, Wang T*, Li H*. Mycobacterium tuberculosis proteasomal ATPase Mpa has a b-grasp domain that hinders docking with the proteasome core protease. Mol Microbiol. 2017 Jul;105(2):227-241. [Epub ahead of print] (: Contributed equally) (*: Correspondence). (cover story).

5. Guan L, He P, Yang F, Zhang Y, Hu YF, Ding JN, Hua Y, Zhang Y, Ye Q, Hu JZ, Wang T*, Jin CW*, Kong DC*. Sap1 is a replication initiation factor essential for the assembly of pre-replicative complex in the fission yeast Schizosaccharomyces pombe. J Biol Chem. 2017.Apr 14;292(15):6056-75. (: Contributed equally) (*: Correspondence). (cover story).

6. Hu K, Geng H, Zhang QZ, Liu QS, Xie MS, Sun CJ, Li WJ, Lin HC, Jiang F, Wang T*, Wu Y-D*, Li ZG*. An in-tether chiral center modulates peptides’ helicity, Cell permeability and target binding affinity. Angew. Chem. Int. Ed. 2016 Jul 4;55(28):8013-7. Epub 2016 May 19. (*: Correspondence).

7. Xu J, Shen C, Wang T*, Quan JM*. Structural basis for the inhibition of Polo-like kinase 1. Nat Struct Mol Biol. 2013 Sep; 20(9):1047-53. Epub 2013 Jul 28. (*: Correspondence). (Highlighted by Nature China).

8. Phan G, Remaut H, Wang T, Allen WJ#, Pirker KF, Lebedev A, Henderson NS, Geibel S, Volkan E, Yan J, Kunze MB, Pinkner JS, Ford B, Kay CW, Li H, Hultgren SJ, Thanassi DG*, Waksman G*. Crystal structure of the FimD usher bound to its cognate FimC-FimH substrate. Nature. 2011 Jun 2;474(7349):49-53. (Article) (: Contributed equally).

9. Wang T, Darwin KH*, Li H*. Binding-induced folding of prokaryotic ubiquitin-like protein on the Mycobacterium proteasomal ATPase targets substrates for degradation. Nat Struct Mol Biol. 2010 Nov; 17(11):1352-7.

10. Wang T, Li H, Lin G, Tang C, Li D, Nathan CF, Darwin KH*, Li H*. Structural insights on the Mycobacterium tuberculosis proteasomal ATPase Mpa. Structure. 2009 Oct14;17(10):1377-85.