Dr. Cao earned his Ph.D. in Pathology from the University of Michigan in 2008. He was a Research Investigator in the Department of Pathology at the University of Michigan before becoming a member of the Houston Methodist Research Institute in 2013. Dr. Cao is currently an affiliate member of the Houston Methodist Research Institute and is Associate Professor of Urology at Northwestern University.

Dr. Cao has been dedicated to characterizing the role of EZH2 in cancer progression. Here is a sampling of his laboratory’s major discoveries:

1-EZH2 transcript and protein levels are consistently elevated in metastatic prostate cancer and aggressive breast carcinoma compared with normal epithelia. EZH2 expression is strongly associated with a metastases- and disease-free prognosis and overall survival.
2-EZH2 regulates several tumor suppressors, including ADRB2, CDH1, rap1GAP, and Slit2. EZH2 overexpression induced epithelial cell invasion and anchorage-independent growth. However, stable EZH2 knockdown inhibited tumor growth of DU145 prostate cancer cells following murine xenograft, indicating EZH2 as a potential therapeutic target for cancer. Companies (e.g., Novartis and GSK) are developing drugs against EZH2.
3-MicroRNA (miR)-101 represses EZH2. miR-101-deficiency yields EZH2 overexpression in cancer, including prostate cancer progression. CGH analysis and genomic DNA qPCR demonstrated that loss of miR-101-encoding genomic regions results in EZH2 overexpression and cancer progression. Dr. Cao was awarded the Department of Defense Prostate Cancer Research Program Fellowship for this work.
4-Dr. Cao discovered a coordinated regulation axis between PRC1 and PRC2, which are elevated in cancer. PRC2 epigenetically regulates miRNAs that repress the PRC1 proteins BMI1 and RING2. These miRNAs play critical roles in tumor growth and cancer stem cell self-renewal. In cancer, EZH2 correlates negatively with PRC2-repressed miRNAs but positively with BMI1, RING2, and their substrate ubiquityl-H2A levels. An epigenetic link between H3K27me3 and ubiquityl-H2A mediated by PRC2-regulated miRNAs was also identified.
5-Mass spectrometric analysis revealed that the PRC2 core protein EED directly interacts with BMI1 and RING1/2. EED-PRC1 interactions attenuate PRC2 histone methyltransferase activities, but enhance PRC1 E3 ubiquitin ligase activities. EED also directly recruits PRC1 to its target genomic loci, suggesting an integral role for EED as an epigenetic exchange factor coordinating PRC1 and PRC2 activities.