Karmanos Cancer Institute
Elliman Building - 1146
421 E. Canfield
Detroit, MI 48201
(1992-1996) Ph.D., University of Texas Health Science Center at Houston and MD Anderson Cancer Center, Houston, TX
(1983-1987) B.S., Jinan University, Guangzhou, China
(1996-2002) Postdoctoral Fellow, California Institute of Technology, Pasadena, California
(2021-Present) Professor, Karmanos Cancer Institute, and Department of Oncology, Wayne State University School of Medicine, Detroit, MI
(2008-2021) Associate Professor, Karmanos Cancer Institute, and Department of Oncology, Wayne State University School of Medicine, Detroit, MI
(2002-2008) Assistant Professor, Karmanos Cancer Institute, and Department of Pathology, Wayne State University School of Medicine, Detroit, MI
Hospital and Other Professional Appointments
(2002-Present) Member, Karmanos Cancer Institute, Detroit, MI
Major Professional Societies
(2016-Present) American Society for Biochemistry and Molecular Biology
(2008-Present) American Society for Microbiology
(2005-Present) American Cancer Society
Honors and Awards
(2013) Wayne State University's President's Research Enhancement Program Award
(2012) Wayne State University GrantPlus Award
(2011) Karmanos Cancer Institute Angelika Burger Award
(2005-2008) Research Scholar Award (American Cancer Society)
(1997-1999) National Research Service Award Postdoctoral Fellowship (NIH)
(1994-1996) Rosalie B. Hite Fellowship (MD Anderson Cancer Center)
(1995) Sowell-Huggins Award (MD Anderson Cancer Center)
(1987) Honor B.S. Degree of Jinan University
CB 7210: Fundamentals of Cancer Biology
CB 7220: Molecular Biology of Cancer Development
CB 7300 F31: Specials Topics in Cancer Biology - Grant Writing
The focus of our research is to understand the molecular mechanisms underlying protein degradation mediated by the ubiquitin-proteasome system (UPS). UPS is the primary intracellular machine responsible for elimination of abnormal proteins and selective destruction of regulatory proteins involved in a wide range of cellular processes including cell cycle control, DNA transcription, replication and repair, and stress response. Dys-regulation of UPS is implicated in various human diseases including cancers. Moreover, UPS has now become an important target for anti-cancer therapy. We use both Saccharomyces cerevisiae and mammalian systems to define the pathways that control the degradation of several key regulatory proteins. In addition, we are studying the differential response of normal cells and cancer cells to the inhibitors of UPS.
1. Ha S-W, Ju D, Hao W, Xie Y (2016) Rapidly translated polypeptides are preferred substrates for cotranslational protein degradation. J Biol Chem 291: 9827-9834.
2. Zhang T, Kho DH, Wang Y, Harazono Y, Nakajima K, Xie Y, Raz A (2015) Gp78, an E3 ubiquitin ligase acts as a gatekeeper suppressing nonalcoholic steatohepatitis (NASH) and liver cancer. PLoS ONE 10: e0118448.
3. Ha S-W, Ju D, Xie Y (2014) Nuclear import factor Srp1 and its associated protein Sts1 couple ribosome-bound nascent polypeptides to proteasomes for cotranslational degradation. J Biol Chem 289: 2701-2710.
4. Wang Y, Ha S-W, Zhang T, Kho D-H, Raz A, Xie Y (2014) Polyubiquitylation of AMF requires cooperation between the gp78 and TRIM25 ubiquitin ligases. Oncotarget 5: 2044-2051.
5. Xie, Y. (2010) Feedback regulation of proteasome gene expression and its implications in cancer therapy. Cancer Metastasis Rev 29: 687-693.
6. Wang, X., Xu, H., Ha, S.W., Ju, D., Xie, Y. (2010) Proteasomal degradation of Rpn4 in Saccharomyces cerevisiae is critical for cell viability under stressed conditions. Genetics 184: 335-342.
7. Ju, D., Wang, X., Xu, H., Xie, Y. (2008) Genome-wide analysis identifies MYND-domain protein Mub1 as an essential factor for Rpn4 ubiquitylation. Mol Cell Biol 28: 1404-1412.
8. Wang, X., Xu, H., Ju, D., Xie, Y. (2008) Disruption of Rpn4-induced proteasome expression in Saccharomyces cerevisiae reduces cell viability under stressed conditions. Genetics 180: 1945-1953.
9. Xu, H., Ju, D., Jarois, T., Xie, Y. (2008) Diminished feedback regulation of proteasome expression and resistance to proteasome inhibitors in breast cancer cells. Breast Cancer Res Treat 107: 267-274.
10. Ju, D., Xie, Y. (2006) Identification of the preferential ubiquitination site and ubiquitin-dependent degradation signal of Rpn4. J Biol Chem 281: 10657-10662.