Hao Dou, Ph.D

Associate professor

Telephone: 86-531-88382190

E-mail: douhao@sdu.edu.cn

Education

Dec. 2013: PhD, Structural Biology, Beatson Institute for Cancer Research (CRUK),Schoolof Medicine,University of Glasgow (UK)

Dec. 2008, Master of Science,Drug Discovery and Translational Biology,School of Biological Science, University of Edinburgh (UK)

June. 2007, Bachelor of Science, Bio-engineering,ChinaPharmaceutical University

Professional Experience

Apr.2014-present Associate Professor at School of Medicine, Shandong University

Awards/Honors

2013 Joseph Black Medal and Hird Prize

2009-2013 PhD Studentship offered by Cancer ResearchUK

2008 Master of Science degree with distinction at University of Edinburgh

Research Interests：

Covalent attachment of ubiquitin to proteins has emerged as an important cellular regulatory mechanism such as cell cycle progression, transcription, protein degradation, DNA repair and virus budding. Defects in these pathways have been associated with diseases such as cancer, neurodegenerative disorder and viral infection. Ubiquitination requires three enzymes, E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme) and E3 (ubiquitin ligase).

I am interested in the molecular mechanism of ubiquitination, specially the structural and functional roles of RING E3s using x-ray crystallography. Cullin-RING ligases (CRLs), the largest family of E3s are involved in cell cycle regulation, signal transduction, DNA repair, gene expression, chromatin remodeling, and embryo developmental process. These complexes contain scaffold protein, RING finger protein, adapter protein and substrate receptor. My research interests focus on CRL4B complex assembled by scaffold protein CUL4B:

lThe role of CRL4B in Hepatitis B virus (HBV) infection: HBx encoded by HBV gene is a small regulatory protein. It plays an important role in the virus life cycle and the pathogenesis of liver cancer.We establish a platform of protein expression, purification, and crystallization. We will study the detailed interactions between CRL4B and HBx for potential antiviral drug design.

lThe role of CRL4B ingenetic transcription: Recently, Prof. Yaoqin Gong’s lab found that CRL4B associates with PRC2 (Polycomb repressive complex 2) and plays a role in transcriptional repression. We will undertake the structural and functional studies of key components from these two complexes and illustrate the mechanism of transcriptional repression at atomic level.

Selected Publications（＊Correspondence）：

1.Dou, H., L. Buetow, G. J. Sibbet, K. Cameron, and D. T. Huang*. (2013). Essentiality of a non-RING element in priming donor ubiquitin for catalysis by a monomeric E3.Nature Structural & Molecular Biology.20 (8):982-989. (Impact factor 12.7)

2.Dou, H., L. Buetow, G. J. Sibbet, K. Cameron, and D. T. Huang*. (2013). BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer.Nature Structural & Molecular Biology.19 (9):876-883. (Impact factor 12.7)

3.Dou, H., L. Buetow, A. Hock, G. J. Sibbet, K. H. Vousden, and D. T. Huang*. (2012). Structural basis for autoinhibition and phosphorylation-dependent activation of c-Cbl.Nature Structural & Molecular Biology.19 (2):184-192. (Impact factor 12.7)

4.Buetow L, Gabrielsen M, Anthony NG,Dou H, Patel A, Aitkenhead H, Sibbet GJ, Smith BO, Huang DT*. (2015). Activation of a Primed RING E3-E2-Ubiquitin Complex by Non-Covalent Ubiquitin. Molecular cell. 58(2):297-310. (Impact factor 14.5) http://dx.doi.org/10.1016/j.molcel.2015.02.017

5.Buetow L, Tria G, Ahmed SF, Hock A,Dou H, Sibbet GJ, Svergun DI, Huang DT*. (2016). Casitas B-lineage lymphoma linker helix mutations found in myeloproliferative neoplasms affect conformation. BMC Biology. 14:76

6.Li PS, Song Y, Zan WY, Qin LP, Han S, Jiang BC,Dou H, Shao CS, Gong YQ*. (2017). Lack of CUL4B in Adipocytes Promotes PPARγ-Mediated Adipose Tissue Expansion and Insulin Sensitivity. Diabetes 66, 300-313

7.Xu X, Liu Q, Zhang C, Ren S, Xu L, Zhao Z,Dou H, Li P, Zhang X, Gong Y, Shaw C*. (2019). Inhibition of DYRK1A-EGFR axis by p53-MDM2 cascade mediates the induction of cellular senescence. Cell Death Dis. 10(4):282