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Faculty Detail    
Name HENGBIN WANG
 
Campus Address KAUL 402A Zip 0024
Phone 205-934-5286
E-mail hbwang@uab.edu
Other websites
     


Faculty Appointment(s)
Appointment Type Department Division Rank
Primary  Biochemistry & Molecular Genetics  Biochemistry & Molecular Genetics Associate Professor
Center  Arthritis & Musculoskeletal Diseases Center  Arthritis & Musculoskeletal Diseases Center Associate Professor
Center  Comprehensive Cancer Center  Comprehensive Cancer Center Associate Professor

Graduate Biomedical Sciences Affiliations
Biochemistry and Molecular Genetics Program 
Biochemistry and Structural Biology 
Cellular and Molecular Biology Program 

Biographical Sketch 
Dr. Hengbin Wang (b.1969) is an Associate Professor of Biochemistry and Molecular Genetics. Dr. Wang received his B.S. degree from Hebei Normal University (1991) and Ph.D. degree from China Agricultural University (1997) in China. He began his first postdoctoral training in Kyushu University, Japan. Then he moved to the University of North Carolina at Chapel Hill, joining Dr. Yi Zhang’s laboratory to study the roles of histone modifications in regulating chromatin functions. He joined UAB in 2004. Currently his laboratory is studying histone ubiquitination and deubiquitination using in vitro and in vivo assays.

Research/Clinical Interest
Title
Role of Histone Modification in Chromatin and cellular Function
Description
In eukaryotic cells, DNA is packaged with histones to form chromatin. Once thought merely as a static structure for DNA compaction, chromatin has now been recognized as being highly dynamic and plays vital regulatory roles in almost all nuclear processes including transcription, replication, repair, recombination, and chromosome segregation. Research during the last ten years revealed that two kinds of activities contribute to chromatin fluidity. One is ATP-dependent nucleosome remodeling; the other is covalent modifications of histone tails. Our lab is particularly interested in how covalent modifications of histone tails regulates chromatin function. Mostly on its N- and C- terminal tails, histones can be covalently modified by acetylation, phosphorylation, methylation, ubiquitination and ADP-ribosylation. Different modifications control different physiological processes. Acetylation plays fundamental roles in transcription regulation. Methylation, depending on the methylation sites and status, modulates a variety of biological processes including transcription, heterochromatin formation, DNA methylation, Gene imprinting, and X chromosome inactivation. The role of histone ubiquitination has just been revealed. We have been focusing our research on two of those modifications: methylation and ubiquitination. We take a series of steps to elucidate the functions of these modifications. First, we will identify novel enzymes responsible for those modifications; second, we will explore functions of those modifications on chromatin-based processes such as transcription; finally we will try to understand the mechanism of those modifications on transcription and further investigate the biological consequences of these modifications. Our long-term goal is to apply this basic research for human diseases.

Selected Publications 
Publication PUBMEDID
Mu Zhang, Shengyan Xiang, Heui-Yun Joo, Lei Wang, Kendra A. Williams, Wei Liu, Chen Hu, Dan Tong, Joshua Haakenson, Chuangui Wang, Shengping Zhang, Ryan E. Pavlovicz, Amanda Jones, Kristina H. Schmidt, Jinfu Tang, Huiqin Dong, Bin Shan, Bin Fang, Peter M. Glazer, Rangasudhagar Radhakrishnan, Patrick Matthias, John Koomen, Edward Seto, Gerold Bepler, Santo V. Nicosia, Jiandong Chen, Chenglong Li, Liya Gu, Guo-Min Li, Wenlong Bai, Hengbin Wang and Xiaohong Zhang. (2014). HDAC6 deacetylates and ubiquitinates MSH2 to maintain proper levels of MutSα. Mol Cell. 2014 Jul 3;55(1):31-46   
Wei Yang, Yun-Hwa Lee, Amanda E. Jones, Jessica L. Woolnough, Dewang Zhou, Qian Dai, Qiang Wu, Keith E. Giles, Tim M. Townes and Hengbin Wang. (2014). The histone H2A deubiquitinase Usp16 regulates embryonic stem cell gene expression and lineage commitment. Nat. Commun 2014 May 2; 5:3818.    
Zhuo Zhang, Amanda E Jones, Heui-Yun Joo, Dewang Zhou, Ying Cao, Shaoxia Chen, Hediye Erdjument-Bromage, Matthew Renfrow, Hang He, Paul Tempst, Tim M Townes, Keith Giles, Ligeng Ma, and Hengbin Wang (2013). USP49 deubiquitinates histone H2B and regulates cotranscriptional pre-mRNA splicing. Genes Dev. Jul 15; 27(14):1581-95.   
Heui-Yun Joo, Ling Zhai, Chunying Yang, Shuyi Nie, Hediye Erdjument-Bromage, Paul Tempst, Chenbei Chang, and Hengbin Wang (2007). Regulation of cell cycle progression and gene expression by H2A deubiquitination. Nature Oct 25; 449, 1068-1072   
Hengbin Wang*, Ling Zhai, Jun Xu, Heui-Yoo Joo, Sarah Jackson, Hediye Erdjument-Bromage, Paul Tempst, Yue Xiong, and Yi Zhang*. (2006). Histones H3 and H4 ubiquitylation by the Cul4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage. Molecular Cell. 22(3):383-394. (*co-correspondence author).   
Hengbin Wang, Liangjun Wang, Migual Vadel, Hediye Erdjument-Bromage, Paul Tempst, Richard S. Jones, and Yi Zhang (2004). Role of H2A ubiquitination in Polycomb gene silencing. Nature 431:873-878.   
Hengbin Wang, An Woojin, Ru Cao, Li Xia, Hediye Erdjument-Bromage, Bruno Chatton, Paul Tempst, Robert G. Roeder, and Yi Zhang (2003). mAM facilitates conversion by ESET of dimethyl to trimethyl lysine 9 of histone H3 to cause transcriptional repression. Molecular Cell, 12 (2), 475-487.   
Hengbin Wang, Ru Cao, Li Xia, Hediye Erdjument-Bromage, Christoph Borchers, Paul Tempst, and Yi Zhang (2001). Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase. Molecular Cell, 8, 1207-1217.   
Hengbin Wang, Zhiqing Huang, Li Xia, Qin Feng, Hediye Erdjument-Bromage, Brain D. Strahl, Scott Briggs, David C. Allis, Jiemin Wong, Paul Tempst, and Yi Zhang (2001). Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclearhormone receptor. Science, 293, 853-857.   

Keywords
epigenetics, histone modifications, ubiquitination and deubiquitination