1985 - 1989 Bachelor of Chemistry, Wuhan University
1989 - 1991 Master of Chemistry, Boston University
1991 - 1996 PhD in Biochemistry, State University of New York at Stony Brook and Cold Spring Harbor Laboratory
1997 - 2002 Postdoctoral Researcher in Biology, California Institute of Technology
2002 - 2020 Assistant Professor, Associate Professor, Professor at University of Texas Health Center
2020 - Present Professor and Head of the Department of Biochemistry, Southern University of Science and Technology
2006 Minority Institution Faculty Scholar Award from the American Cancer Society
1998-2001 Postdoctoral Award from the American Leukemia Foundation
1996 Doctoral Research Award from the State University of New York at Stony Brook
Research
Protein homeostasis and its impact on health and disease Mechanisms of protein degradation induced by ubiquitination and its regulation Development of new cancer therapies through protein stability manipulation Role of ubiquitination in aging and neurodegenerative diseases
Synthesis and characterization of a 29-amino acid residue DNA-binding peptide derived from a/b-type small acid soluble spore proteins (SASP) of bacteria, Rao, H., Mohr, S.C., Fairhead, H. and Setlow, P., 1992
The replicon model and eukaryotic chromosomes, Bell, S.P., Marhrens, Y., Rao, H. and Stillman, B., 1993
Functional conservation of modular elements in yeast chromosomal replicators, Rao, H., Marhrens, Y. and Stillman, B., 1994
The origin recognition complex (ORC) interacts with a bipartite DNA binding site within yeast replicators, Rao, H. and Stillman, B., 1995
Degradation of a cohesin subunit by the N-end rule pathway is essential for chromosome stability, Rao, H., Uhlmann, F., Nasmyth, K. and Varshavsky, A., 2001
Recognition of specific ubiquitin conjugates is important for the proteolytic functions of the UBA domain proteins Dsk2 and Rad23, Rao, H.* and Sastry, A., 2002
Multiple interactions of Rad23 suggest a mechanism for ubiquitylated substrate delivery important in proteolysis, Kim, I., Mi, K. and Rao, H., 2004
Analysis of Ub-binding proteins by yeast two-hybrid, Apodaca, J., Ahn, J.M., Kim, I. and Rao, H., 2005
The Png1-Rad23 complex regulates glycoprotein turnover, Kim, I., Ahn, J., Liu, C., Tanabe, K., Apodaca, J., Suzuki, T. and Rao H., 2006
What’s Ub chain linkage got to do with it?, Kim, I. and Rao, H., 2006
Cellular tolerance of prion in yeast requires the unfolded protein response and proteolysis, Apodaca, J., Kim, I. and Rao, H., 2006
Proteasome inhibition in wild-type yeast Saccharomyces cerevisiae cells, Liu, C., Apodaca, J., Davis, L.E. and Rao, H., 2007
A genome-wide synthetic dosage lethality screen reveals multiple pathways that require the functioning of Ub-binding proteins Rad23 and Dsk2, Liu, C., van Dyk, D., Li, Y., Andrews, B. and Rao, H., 2009
Usa1 protein facilitates substrate ubiquitylation through two separate domains, Kim, I., Li, Y., Muniz, P. and Rao, H., 2009
Rad4 regulates protein turnover at a postubiquitylation step, Li, Y., Yan, J., Kim, I., Liu, C., Huo, K. and Rao, H., 2010
Degradation of misfolded secretory and membrane proteins and associated diseases, Kim, I., and Rao, H., 2010
Ubiquitin chain elongation enzyme Ufd2 regulates a subset of Doa10 substrates, Liu, C., van Dyk, D., Xu, P., Choe, V., Pan, H., Peng, J., Andrews, B. and Rao, H., 2010
Identification of an Htm1 (EDEM)- dependent, Mns1-independent Endoplasmic Reticulum-associated Degradation (ERAD) pathway in Saccharomyces cerevisiae: application of a novel assay for glycoprotein ERAD, Hosomi, A., Tanabe, K., Hiryama, H., Kim, I., Rao, H. and Suzuki, T., 2010
Genome-wide approaches to systematically identify substrates of the ubiquitin-proteasome pathway, Liu, C., Choe, V. and Rao, H., 2010
A newly identified Pirh2 substrate SCYL-1-BP1 can bind to MDM2 and accelerate MDM2 self-ubiquitination, Yan, J., Zhang, D., Di, Y., Shi, H., Rao, H. and Huo, K., 2010
Overexpression of SCYL1-BP1 stabilizes functional p53 suppressing MDM2-mediated ubiquitination, Yan, J., Di, Y., Shi, H., Rao, H. and Huo K., 2010
The Cdc48 ATPase modulates the interaction between two proteolytic factors Ufd2 and Rad23, Baek, G.H., Kim, I., and Rao, H., 2011
Ubiquitin ligase Ufd2 is required for efficient degradation of Mps1 kinase, Liu, C., van Dyk, D., Choe, V., Yan, J., Majumder, S., Costanzo, M., Bao, B., Boone, C., Huo, K. Winey, M., Fisk, H., Andrews, B. and Rao, H., 2011
The Cdc48 and its cofactor Vms1 are involved in Cdc13 protein degradation, Baek, G.H., Cheng, H., Kim, I., and Rao, H., 2012
Cdc48, a swiss army knife of cell biology, Baek, G.H., Cheng, H., Choe, V., Bao, X., Shao, J., Luo, S., and Rao, H., 2013
XPC promotes MDM2-mediated degradation of the p53 tumor suppressor, Krzeszinski, J., Choe, V., Shao, J., Bao, X., Cheng, H., Luo, S., Huo, K., and Rao, H., 2014
Unglycosylated prion PrP for ubiquitylation and degradation, Shao, J., Choe, V., Cheng, H., Tsai, C., Weissman, A., Luo , S. Rao, H., 2014
Down-regulation of Gli transcription factor leads to the inhibition of migration and invasion of ovarian cancer cells via integrin β4-mediated FAK signaling, Chen, Q., Xu, R., Zeng, C., Lu, Q., Huang, D, Shi, C., Yan, R., Zhang, W., Deng, L., Rao, H., Gao, G., Luo, S., 2014
Heat shock protein 90 beta stabilizes Focal Adhesion Kinase and enhances cell migration and invasion in breast cancer cells, Xiong, X., Wang, Y., Liu, C., Lu, Q., Liu, T. Chen, G., Rao, H., Luo, S., 2014
Rad25 protein is targeted for degradation by the Ubc4-Ufd4 pathway, Bao, X., Johnson, J., and Rao, H., 2015
Inhibition of Hedgehog signaling pathway impedes cancer cell proliferation by promotion of autophagy, Tang, X., Deng, L., Chen, Q, Wang, Y., Xu, R., Shi, C., Shao, J., Hu, G., Gao, M., Rao, H., Luo, S., Lu, Q., 2015
Guidelines for the Use and Interpretation of Assays for Monitoring Autophagy, Klionsky, A. et al., 2016
The F box protein Rcy1 is involved in the degradation of Histone variant Cse4 and genome maintenance, Cheng, H., Bao, X., and Rao, H, 2016
Nek2A phosphorylates and stabilizes SuFu: A new strategy of Gli2/Hedgehog signaling regulatory mechanism, Wang Y, Li Y, Hu G, Huang X, Rao H, Xiong X, Luo Z, Lu Q, Luo S., 2016
