饶海生物化学系主任、教授、博士生导师


raoh@sustech.edu.cn
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个人简介南方科技大学医学院教授，生物化学系主任，博士生导师。曾任德克萨斯大学健康中心教授，着重研究蛋白质稳态调控的机理和功能。培养40多名学生，博士，博士后。研究长期被美国NIH，癌症协会，国防部及多个私人基金会支持。担任多个国际基金评审专家和学术杂志编委。课题组的研究在多个国际杂志发表包括Nature，PNAS，JCB，JBC，BMC，Cancer Research，Scientific Reports等等。
研究领域蛋白质稳态在健康和疾病功能影响。蛋白质稳态和质量控制对细胞的正常生命活动至关重要。蛋白质稳态异常导致多种疾病，包括肿瘤和神经退行性疾病。实验室主要利用酵母菌和人的细胞体系, 开展蛋白质修饰和泛素化引起蛋白质降解的机理研究。在此基础上，我们将研究蛋白质稳态调控机制及其在多项疾病包括癌症和老年神经性疾病中的作用。具体研究方向有以下：
1）利用酵母菌做大规模的筛选与蛋白质稳态调控疾病有关的基因。
2）蛋白质泛素化是如何调控细胞内各种通路（包括DNA修复，细胞周期调控，自噬autophagy等等）。蛋白质泛素化裂解的一个最重要的作用就是帮助细胞迅速适应新挑战和变化，比如DNA伤害，细胞周期变化和各种stress。我们一直在关注蛋白质裂解在这些方面的贡献，有一定的经验和基础，也将做筛选来确定其功能和影响。
3）蛋白质泛素化技术应用，发展新的治癌药物和治疗方法。我们已经在设计新方法把导致人体疾病的蛋白质快速降解，来开发其治疗效应。
4）泛素化如何通过调控蛋白质的质量而可能参与老年神经性疾病的发展。我们在这方面已有一定的基础，对多个有折叠错误而被裂解多蛋白有深刻的研究。



教育背景1985 - 1989 武汉大学 化学 学士；
1989 - 1991 波士顿大学 化学 硕士；
1991 - 1996 纽约州立大学石溪分校及冷泉港实验室 生物化学 博士



工作经历1997 - 2002 加州理工学院 生物 博士后；
2002 - 2020 德克萨斯大学健康中心 助理教授，（终生）副教授，（终生）教授；
2020 - 现在 南方科技大学医学院 教授、生物化学系主任



获奖情况及荣誉2006年 美国 癌症研究协会少数族裔院校教授****奖
1998-2001年 美国白血病基金会 博士后奖
1996年 纽约州立大学石溪分校博士生研究奖



杂志编委会成员多个国际杂志的编委 包括 J. Biol. Chem.; Frontiers in Cell and Developmental Biology and Oncology; Adv. In Biol.,; J. Membrane Sci. Tech.
在德克萨斯大学担任各级院校研究生及教授委员会委员



近年代表文章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.
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.
Rao, H., Marhrens, Y. and Stillman, B. (1994) Functional conservation of modular elements in yeast chromosomal replicators. Mol. Cell. Biol. 14: 7643-7651.
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.
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.
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.
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
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.
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.
Kim, I. and Rao, H. (2006) What’s Ub chain linkage got to do with it? Science STKE 330: pe18.
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.
Liu, C., Apodaca, J., Davis, L.E. and Rao, H. (2007) Proteasome inhibition in wild-type yeast Saccharomyces cerevisiae cells. Biotechniques 42: 158-162.
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 **
Kim, I., Li, Y., Muniz, P. and Rao, H. (2009) Usa1 protein facilitates substrate ubiquitylation through two separate domains. PLos One 4: e7604. PMCID: PMC**
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: PMC**
Kim, I., and Rao, H. (2010) Degradation of misfolded secretory and membrane proteins and associated diseases. eLS doi 10.1002/02.a**
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 **
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: PMC**
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 **
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: PMC**
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.
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: PMC**
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: PMC**
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: PMC**
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.
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.
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.
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.
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.
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: PMC**
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.
Klionsky, A. et al. (2016) Guidelines for the Use and Interpretation of Assays for Monitoring Autophagy Autophagy 12, 1-222. PMID: **
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.
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: **.
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.
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: **
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: **
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: **
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
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
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
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.