professor School of Medicine

Professor, Department of Biochemistry, School of medicine, Southern University of science and technology. He was a professor at the University of Texas Health Center, focusing on the mechanism and function of protein homeostasis regulation. He trained more than 40 students, doctors and postdoctors. The research has long been supported by NIH, cancer society, Department of defense and several private foundations. As a number of international fund review experts and editorial board members of academic journals. Our research has been published in many international journals, including nature, PNAs, JCB, JBC, BMC, cancer research, scientific reports, etc.

Personal Profile

Research

Protein homeostasis plays an important role in health and disease function. Protein homeostasis and quality control are crucial to the normal life of cells. Abnormal protein homeostasis leads to a variety of diseases, including tumors and neurodegenerative diseases. The mechanism of protein degradation induced by protein modification and ubiquitination was studied by yeast and human cell system. On this basis, we will study the regulation mechanism of protein homeostasis and its role in a number of diseases, including cancer and senile neurological diseases. The specific research directions are as follows:

1) Large scale screening of genes related to protein homeostasis in yeast.

2) How protein ubiquitination regulates various intracellular pathways (including DNA repair, cell cycle regulation, autophagy, etc.). One of the most important functions of protein ubiquitination is to help cells adapt to new challenges and changes, such as DNA damage, cell cycle changes and various stresses. We have been paying attention to the contribution of protein cleavage in these aspects. We have some experience and foundation, and will also do screening to determine its function and impact.

3) Protein ubiquitination technology application, the development of new cancer drugs and treatment methods. We are already designing new methods to rapidly degrade proteins that cause human diseases to develop their therapeutic effects.

4) How can ubiquitination participate in the development of senile neurological diseases by regulating the quality of proteins. We have a certain foundation in this area, and have a deep research on the cleaved proteins with folding errors.


Publications Read More

  1. Rao, H., Mohr, S.C., Fairhead, H. and Setlow, P. (1992) 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. FEBS Ltr. 305: 115-120.
  2. Bell, S.P., Marhrens, Y., Rao, H. and Stillman, B. (1993) The replicon model and eukaryotic chromosomes. Cold Spring Harbor Symp. Quant. Biol. 58: 435-442.
  3. Rao, H., Marhrens, Y. and Stillman, B. (1994) Functional conservation of modular elements in yeast chromosomal replicators. Mol. Cell. Biol. 14: 7643-7651.
  4. Rao, H. and Stillman, B. (1995) The origin recognition complex (ORC) interacts with a bipartite DNA binding site within yeast replicators. Proc. Natl. Acad. Sci. USA 92: 2224-2228.
  5. Rao, H., Uhlmann, F., Nasmyth, K. and Varshavsky, A. (2001) Degradation of a cohesin subunit by the N-end rule pathway is essential for chromosome stability. Nature 410: 955-959.
  6. Rao, H.* and Sastry, A. (2002) Recognition of specific ubiquitin conjugates is important for the proteolytic functions of the UBA domain proteins Dsk2 and Rad23. J. Biol. Chem. 277: 11691-11695.
  7. Kim, I., Mi, K. and Rao, H. (2004) Multiple interactions of Rad23 suggest a mechanism for ubiquitylated substrate delivery important in proteolysis. Mol. Biol. Cell. 15: 3357-3365. PMCID: PMC452589
  8. Apodaca, J., Ahn, J.M., Kim, I. and Rao, H. (2005) Analysis of Ub-binding proteins by yeast two-hybrid. Methods Enzymol. 399: 157-64.
  9. Kim, I., Ahn, J., Liu, C., Tanabe, K., Apodaca, J., Suzuki, T. and Rao H. (2006) The Png1-Rad23 complex regulates glycoprotein turnover. J. Cell Biol. 172: 211-219.
  10. Kim, I. and Rao, H. (2006) What’s Ub chain linkage got to do with it? Science STKE 330: pe18.
  11. Apodaca, J., Kim, I. and Rao, H. (2006) Cellular tolerance of prion in yeast requires the unfolded protein response and proteolysis. Biochem. Biophys. Res. Commun. 347: 319-326.
  12. Liu, C., Apodaca, J., Davis, L.E. and Rao, H. (2007) Proteasome inhibition in wild-type yeast Saccharomyces cerevisiae cells. Biotechniques 42: 158-162.
  13. Liu, C., van Dyk, D., Li, Y., Andrews, B. and Rao, H. (2009) A genome-wide synthetic dosage lethality screen reveals multiple pathways that require the functioning of Ub-binding proteins Rad23 and Dsk2. BMC Biol. 7: 75. PMCID: PMC 2777868
  14. Kim, I., Li, Y., Muniz, P. and Rao, H. (2009) Usa1 protein facilitates substrate ubiquitylation through two separate domains. PLos One 4: e7604. PMCID: PMC2764048
  15. Li, Y., Yan, J., Kim, I., Liu, C., Huo, K. and Rao, H. (2010) Rad4 regulates protein turnover at a postubiquitylation step. Mol. Biol. Cell. 21: 177-185. PMCID: PMC2801711
  16. Kim, I., and Rao, H. (2010) Degradation of misfolded secretory and membrane proteins and associated diseases. eLS doi 10.1002/9780470015902.a0022577
  17. Liu, C., van Dyk, D., Xu, P., Choe, V., Pan, H., Peng, J., Andrews, B. and Rao, H. (2010) Ubiquitin chain elongation enzyme Ufd2 regulates a subset of Doa10 substrates. J. Biol. Chem. 285: 10265-10272. PMCID: PMC 2856231
  18. Hosomi, A., Tanabe, K., Hiryama, H., Kim, I., Rao, H. and Suzuki, T. (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. J. Biol. Chem. 285: 24324-24334. PMCID: PMC2915668
  19. Liu, C., Choe, V. and Rao, H. (2010) Genome-wide approaches to systematically identify substrates of the ubiquitin-proteasome pathway. Trends Biotechnol. 28: 461-467. PMCID: PMC 2926183
  20. Yan, J., Zhang, D., Di, Y., Shi, H., Rao, H. and Huo, K. (2010) A newly identified Pirh2 substrate SCYL-1-BP1 can bind to MDM2 and accelerate MDM2 self-ubiquitination. FEBS Lett. 584: 3275-3278. PMCID: PMC3798065
  21. Yan, J., Di, Y., Shi, H., Rao, H. and Huo K. (2010) Overexpression of SCYL1-BP1 stabilizes functional p53 suppressing MDM2-mediated ubiquitination. FEBS Lett. 584: 4319-4324.
  22. Baek, G.H., Kim, I., and Rao, H. (2011) The Cdc48 ATPase modulates the interaction between two proteolytic factors Ufd2 and Rad23. PNAS 108:13558-63. PMCID: PMC3158229
  23. 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) Ubiquitin ligase Ufd2 is required for efficient degradation of Mps1 kinase. J. Biol. Chem 286: 43660-43667. PMCID: PMC3243506
  24. Baek, G.H., Cheng, H., Kim, I., and Rao, H. (2012) The Cdc48 and its cofactor Vms1 are involved in Cdc13 protein degradation. J. Biol. Chem 287: 26788-26795. PMCID: PMC3411016
  25. Baek, G.H., Cheng, H., Choe, V., Bao, X., Shao, J., Luo, S., and Rao, H. (2013). Cdc48, a swiss army knife of cell biology. J. Amino Acids 2013, doi 10.1155/2013/183421.
  26. Krzeszinski, J., Choe, V., Shao, J., Bao, X., Cheng, H., Luo, S., Huo, K., and Rao, H. (2014) XPC promotes MDM2-mediated degradation of the p53 tumor suppressor. Mol. Biol. Cell. 25, 213-221.
  27. Shao, J., Choe, V., Cheng, H., Tsai, C., Weissman, A., Luo , S. Rao, H. (2014) Ubiquitin ligase gp78 targets unglycosylated prion PrP for ubiquitylation and degradation. PLos One e92290.
  28. 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) Down-regulation of Gli transcription factor leads to the inhibition of migration and invasion of ovarian cancer cells via integrin β4-mediated FAK signaling. PLos One e88386.
  29. Xiong, X., Wang, Y., Liu, C., Lu, Q., Liu, T. Chen, G., Rao, H., Luo, S. (2014) Heat shock protein 90 beta stabilizes Focal Adhesion Kinase and enhances cell migration and invasion in breast cancer cells. Exp. Cell Res. 326: 78-89.
  30. Bao, X., Johnson, J., and Rao, H. (2015) Rad25 protein is targeted for degradation by the Ubc4-Ufd4 pathway. J. Biol. Chem 290, 8606-8612. PMCID: PMC4375509
  31. 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) Inhibition of Hedgehog signaling pathway impedes cancer cell proliferation by promotion of autophagy. Euro. J. Cell Biol., 94:223-233.
  32. Klionsky, A. et al. (2016) Guidelines for the Use and Interpretation of Assays for Monitoring Autophagy Autophagy 12, 1-222. PMID: 26799652
  33. Cheng, H., Bao, X., and Rao, H (2016) The F box protein Rcy1 is involved in the degradation of Histone variant Cse4 and genome maintenance. J. Biol. Chem 291: 10372-10377.
  34. Wang Y, Li Y, Hu G, Huang X, Rao H, Xiong X, Luo Z, Lu Q, Luo S. (2016) Nek2A phosphorylates and stabilizes SuFu: A new strategy of Gli2/Hedgehog signaling regulatory mechanism. Cellular signaling 28:1304-13. PMID: 27297360.
  35. Zhou F, Huang D, Li Y, Hu G, Rao H, Lu Q, Luo S, Wang Y. (2017) Nek2A/SuFu feedback loop regulates Gli- mediated Hedgehog signaling pathway. Int J Oncol. 50, 373-380.
  36. Shao J., Xu L., Chen L., Lu Q., Xie X., Shi W., Xiong W., Shi C., Huang X., Mei J., Rao H, Lu H., Lu N., Luo S. (2017) The small G-protein Arl13b promotes gastric tumorigenesis by regulating Smoothened trafficking and subsequent Hedgehog signaling pathway activation. Cancer Research 77: 4000-4013. PMID: 28611043
  37. Peng H, Yang J, Li G, You Q, Han W, Li T, Gao D, Xie X, Lee BH, Du J, Hou J, Zhang T, Rao H, Huang Y, Li Q, Zeng R, Hui L, Wang H, Xia Q, Zhang X, He Y, Komatsu M, Dikic I, Finley D, Hu R. (2017) Ubiquitylation of p62/sequestosome1 activates its autophagy receptor function and controls selective autophagy upon ubiquitin stress. Cell Res. 27: 657-674. PMID: 28322253
  38. Cheng, H., Bao, X., Gan, X., Luo, S. and Rao, H (2017) Multiple E3s promote the degradation of Histone variant Cse4. Scientific Reports 7: 8565. PMID: 28819127
  39. Hu, G., Luo, S., Cheng, H., Gan, X., and Rao, H (2018) A simple PCR-based strategy for the introduction of point mutations in the yeast S. cerevisiae via CRISPR/CAS9. Biochem Mol Biol J. 4: 9. DOI: 10.21767/2471-8084.100058
  40. Shanmugasundarum, K., McHardy, S., Luo, T., and Rao, H. (2019) A modular PROTAC design for target destruction using a degradation signal based on single amino acids. J. Biol. Chem 294: 15172
  41. Yan, Z., Luo, S and Rao, H. (2020) The N-terminal domain of ABL confers protein instability and supresses tumorigenesis. J. Biol. Chem 295: 10.1074/jbc.RA120.012821
  42. Hu, G., Yan, Z., Rios, L., Jasper A., Luo, S. and Rao, H. (2020)  Autophagy regulator Atg9 is degraded by the proteasome. Biochem. Biophys. Res. Commun. 522: 254-8.

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Contact Address

South University of science and technology,Shenzhen

Office Phone

075588018248

Email

raoh@sustech.edu.cn

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