Faculty Profiles Department of Pathology

Xiaohong (Mary) Zhang, Ph.D.
Assistant Professor
Department of Pathology and Cell Biology
MDC BOX-11
Tampa, FL-33612
(813) 974-1288
Email: Xiaohong Zhang
Office: MDC 2108
Lab: MDC 2023

Year Appointed: 2006

Research/Interest:
Ovarian Cancer

Research Description

•Post-translational modifications, such as phosphorylation and acetylation, play important roles in a variety of cellular processes. Alterations of these modifications may lead to human diseases including cancer. Our lab is interested in how these post-translational modifications, particularly how acetylation, influences biological functions such as gene expression, cell motility etc., in normal and aberrant settings. Our ultimate goal is to apply our knowledge to cure human diseases.

Basic research:

•Studies in our lab focus on one of the class II histone deacetylases (HDACs), HDAC6. HDAC6 is unique within the HDAC family. It has two HDAC domains and deacetylates both histone and tubulin, suggesting it plays important roles in both nuclei and cytoplasm. To study the function of HDAC6 systematically, we plan to purify HDAC6 complex from nuclei and cytoplasm. The outcome of this study will reveal the biological functions of this HDAC.

Translational research:

•Our lab is interested in studying the role of HDAC6 and its novel substrate, cortactin, in human cancers, particularly in ovarian and breast cancers. Our previous investigation showed that HDAC6 and cortactin are associated with cell migration. We will further determine whether HDAC6 and cortactin, especially the deacetylated form of cortactin, are involved in ovarian and breast cancer metastasis.

Representative Publications :

•Zhang, X., Yuan, Z., Zhang, Y., Yong, S., Salas-Burgos, A., Koomen, Olashaw, N., Parsons, J.T. Yang, X-J., Dent, S.R., Yao, T-P, Lane, W.S. and T-P, Yao, and Seto, E. (2006) HDAC6 modulates cell motility by altering the acetylation level of cortactin (under reviewed in Cell)

•Zhang, X., Ozawa, Y., Lee H., Wen, Y-D., Tan, T-H, Wadzinski, B.E. and Seto, E. (2005) Histone deacetylase 3 (HDAC3) activity is regulated by interaction with protein serine/threonine phosphatase 4. Genes & Dev. 19, 827-839

•Zhang, X., Wharton, W., Yuan, Z., Tsai, S-C., Olashaw, N., and Seto, E. (2004) Activation of the growth/differentiation factor 11 gene by the histone deacetylase inhibitor trichostatin A and repression by HDAC3. Mol. Cell. Biol. 24, 5106-5118


	Xiaohong (Mary) Zhang, Ph.D. Assistant Professor Department of Pathology and Cell Biology MDC BOX-11 Tampa, FL-33612 (813) 974-1288 Email: Xiaohong Zhang Office: MDC 2108 Lab: MDC 2023 Year Appointed: 2006
	Research/Interest: Ovarian Cancer Research Description •Post-translational modifications, such as phosphorylation and acetylation, play important roles in a variety of cellular processes. Alterations of these modifications may lead to human diseases including cancer. Our lab is interested in how these post-translational modifications, particularly how acetylation, influences biological functions such as gene expression, cell motility etc., in normal and aberrant settings. Our ultimate goal is to apply our knowledge to cure human diseases. Basic research: •Studies in our lab focus on one of the class II histone deacetylases (HDACs), HDAC6. HDAC6 is unique within the HDAC family. It has two HDAC domains and deacetylates both histone and tubulin, suggesting it plays important roles in both nuclei and cytoplasm. To study the function of HDAC6 systematically, we plan to purify HDAC6 complex from nuclei and cytoplasm. The outcome of this study will reveal the biological functions of this HDAC. Translational research: •Our lab is interested in studying the role of HDAC6 and its novel substrate, cortactin, in human cancers, particularly in ovarian and breast cancers. Our previous investigation showed that HDAC6 and cortactin are associated with cell migration. We will further determine whether HDAC6 and cortactin, especially the deacetylated form of cortactin, are involved in ovarian and breast cancer metastasis. Representative Publications : •Zhang, X., Yuan, Z., Zhang, Y., Yong, S., Salas-Burgos, A., Koomen, Olashaw, N., Parsons, J.T. Yang, X-J., Dent, S.R., Yao, T-P, Lane, W.S. and T-P, Yao, and Seto, E. (2006) HDAC6 modulates cell motility by altering the acetylation level of cortactin (under reviewed in Cell) •Zhang, X., Ozawa, Y., Lee H., Wen, Y-D., Tan, T-H, Wadzinski, B.E. and Seto, E. (2005) Histone deacetylase 3 (HDAC3) activity is regulated by interaction with protein serine/threonine phosphatase 4. Genes & Dev. 19, 827-839 •Zhang, X., Wharton, W., Yuan, Z., Tsai, S-C., Olashaw, N., and Seto, E. (2004) Activation of the growth/differentiation factor 11 gene by the histone deacetylase inhibitor trichostatin A and repression by HDAC3. Mol. Cell. Biol. 24, 5106-5118