Division of Life Science
 
  • About
       
  • News & Events
 
  • Division Intranet
 

Mingjie ZHANG

PhD Calgary
Kerry Holdings Professor of Science
Member, Chinese Academy of Science

Email: mzhang@ust.hk

Laboratory Homepage

Research Interests
Structural biology of neuronal signaling complex organization and regulation; protein complexes governing cell polarity; screening and development of small molecules with therapeutic potentials.

Representative Publications

For a complete list of the publications with full PDF version, please visit Mingjie Zhang’s Lab Homepage.
 

1.     Wang, C., Yu, C., Ye, F., Wei, Z., and Zhang, M. (2012) “Structure of the ZU5-ZU5-UPA-DD supramodule of ankyrin-B reveals interaction surfaces necessary for ankyrin function” PNAS (in press).
 

2.     Zhu, J., Shang, Y., Xia, C., Wang, W., Wen, W., and Zhang, M. (2011) “Guanylate Kinase Domains of the MAGUK Family Scaffold Proteins as Specific Phospho-Protein Binding ModulesEMBO J 30, 4986 - 4997.

 

3.     Wei, Z., Zheng, S., Spangler, S. A., Yu, C., Hoogenraad, C. C., and Zhang, M. (2011) “Liprin-mediated Large Signaling Complex Organization Revealed by the Liprin-a/CASK and Liprin-a/Liprin-b Complex Structures” Mol Cell 43, 586-598.
  

4.     Zhu, J., Wen, W., Zheng, Z., Shang, S., Wei, Z., Xiao, Z., Pan, Z., Du, Q., Wang, W., and Zhang, M. (2011) “LGN/mInsc and LGN/NuMA Complex Structures Suggest Distinct Functions in Asymmetric Cell Division for the Par3/mInsc/LGN and Gαi/LGN/NuMA Pathways” Mol Cell 43, 418-431.
  

5.     Liu, W., Wen, W., Wei, Z., Yu, J., Ye, F., Liu, C-H., Hardie, R. C., and Zhang, M. (2011) “The INAD scaffold is a dynamic, redox-regulated modulator of signalling in the Drosophila eyeCell 145, 1088-1101. [Cover article].
  

6.     Wu, L., Pan, L., Wei, Z., and Zhang, M. (2011) “Structure of MyTH4-FERM Domains in Myosin VIIa Tail Bound to CargoScience 331, 757-760.
  

7.     Wei, Z., Yan, J., Pan, L. Lu, Q., and Zhang, M. (2011) “Cargo Recognition Mechanism of Myosin X Revealed by the Structure of its Tail MyTH4-FERM Tandem in Complex with the DCC P3 Domain” PNAS 108, 3572-3577.
  

8.     Huo, L., Wen, W., Wang, R., Kam, C., Xia, J., Feng, W., and Zhang, M. (2011) “Cdc42-dependent formation of the ZO-1/MRCKb complex at the leading edge controls cell migration EMBO J 30, 665-678.
  

9.      Yan, J., Pan L. F., Chen, X., Wu, L., and Zhang, M. (2010) “The Structure of the Harmonin/Sans Complex Reveals an Unexpected Interaction Mode of the Two Usher Syndrome Proteins”. PNAS 107, 4040-4045.
 

10.  Wen, W., Yu, J., Pan, L., Weng, J., Wang, W., Ong, Y. S., Tran, T. H., Hong, W. and Zhang, M. (2010) “Lipid-induced Conformational Switch Controls Fusion Activity of Longin Domain SNARE Ykt6”. Mol Cell 37, 383-395.
  

11.  Yu, C., Feng, W., Wei, Z., Miyanoiri, Y., Wen, W., Zhao, Y., and Zhang, M. (2009) “Myosin VI undergoes cargo-mediated dimerization” Cell 138, 537-548.
  

12.  Wang, R., Wei, Z., Jin, H., Wu, H., Yu, C., Wen, W., Chan, L.-N., Wen, Z., and Zhang, M. (2009) “Auto-inhibition of UNC5b Revealed by the Cytoplasmic Domain Structure of the Netrin Receptor” Mol Cell  33, 692-703.
  

13.  Feng, W., and Zhang, M. (2009). Organization and dynamics of PDZ domain-related supramodules in the postsynaptic density. Nat. Rev. Neurosci. 10: 87-99.
  

14.  Pan L. F., Yan, J., Wu, L., and Zhang, M. (2009). Assembling stable hair cell tip link complex via multi-dentate interactions between Harmonin and Cadherin23. Proc. Natl. Acad. Sci. 106: 5575-5580.
 
 

15.  Chen, J., Pan, L. F., Wei, Z., Zhao, Y., and Zhang, M. (2008). Domain swapped dimerization of ZO-1 PDZ2 generates specific and regulatory connexin43 binding
sites. EMBO J. 27: 2113-2123.
 

16.  Wu, H, Feng, W., Chen, J., Chan, L.-N., Huang, S., and Zhang, M. (2007) “PDZ Domains of Par-3 as Potential Phosphoinositide Signaling Integrators” Mol Cell 28, 886-898.
 

17.  Pan, L. F., Wu, H., Shen, C., Shi, Y., Jin, W., Xia, J., and Zhang, M. (2007) “Clustering and synaptic targeting of PICK1 requires direct interaction between the PDZ domain and lipid membranes” EMBO J 26, 4576-4587.
  

18.  Feng, W., Wu, H., Chan, L.-N., and Zhang, M. (2007). The Par-3 NTD adopts a PB1- like structure required for Par-3 oligomerization and apical membrane localization. EMBO J. 26: 2786-2796.
 

19.  Feng, W., Long, J., and Zhang, M. (2005). A unified assembly mode revealed by the structures of tetrameric L27 domain complexes formed by mLin-2/mLin-7 and Patj/Pals1 scaffold proteins. Proc. Natl. Acad. Sci. U.S.A. 102: 6861-6866.
  

20.  Long, J.-F., Feng, W., Wang, R., Chan, L.-N., Ip, F.C.F., Xia, J., Ip, N., and Zhang, M. (2005). Auto-inhibition of X11s/Mints scaffold proteins revealed by the closed conformation of the PDZ tandem. Nat. Struct. Mol. Biol. 12: 722-728.
  

21.  Yan, J., Wen, W., Xu, W., Long, J.-F., Adams, M. E., Froehner, S.C., and Zhang, M. (2005). Structure of the Split PH domain and distinct lipid binding properties of the PH-PDZ supramodule of a1-Syntrophin. EMBO J. 24: 3985-3995.
  

22.  Feng, W., Long, J., Fan, J.-S., Tetsuya, S., and Zhang, M. (2004). Hetero-tetrameric L27 (Lin-2, Lin-7) domain complexes as organization platforms for supra-molecular assemblies. Nat. Struct. Mol. Biol. 11: 475-480.
  

23.  Feng, W., Shi, Y., Li, M., and Zhang, M. (2003). Tandem PDZ repeats in glutamate receptor interacting proteins have a novel mode of PDZ domain-mediated target binding. Nat. Struct. Biol. 10: 972-978.
  

24.  Zhang, M., and Wang, W. (2003). Organization of signaling complexes by PDZ-domain scaffold proteins. Acc. Chem. Res. 36: 530-538.
  

25.  Tochio, T., Tsui, M. M. K., Banfield, D. K., and Zhang, M. (2001). An auto-inhibitory mechanism for non-syntaxin SNARE proteins revealed by the structure of Ykt6p. Science 293: 698-702.
  

26.  Tochio, H., Zhang, Q., Mandal, P., Li., M., and Zhang, M. (1999). Solution structure of the extended neuronal nitric oxide synthase PDZ domain complexed with an associated peptide. Nat. Struct. Biol. 6: 417-421.
  

27.  Zhang, M., Tanaka, T., and Ikura, M. (1995). Calcium-induced conformational transition revealed by the solution structure of Apo Calmodulin. Nat. Struct. Biol. 2: 758-767.

 

< Back