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Biochemistry Department - Primary Faculty

Hung-Ying Kao, Ph.D.

Associate Professor

Education

  • Ph.D.: University of Minnesota, 1996
  • Postdoc: The Salk Institute for biological studies, 2001

Research Interests

Our lab is interested in transcriptional regulation in human health and diseases. Currently, we have three ongoing projects:

  • 1. Characterizing the biological function of histone deacetylase 7 (HDAC7) and its interacting proteins including alpha actinin 4 (ACTN4).
    HDAC7 is a member of class II HDACs. Precise regulation of the subcellular distribution of class II HDACs plays a pivotal role in cell differentiation and animal development. ACTN4 is an HDAC7 interacting protein and mutations in ACTN4 are associated with focal segmental glomerulosclerosis (FSGS), a kidney disease characterized by proteinuria. We are investigating the function and regulation of HDAC7 and ACTN4 in endothelial cells and podocytes.
  • 2. Elucidating the mechanisms underlying tamoxifen-resistant breast cancer.
    The selective estrogen receptor modulator (SERM) tamoxifen is an important agent in the treatment of ER-positive breast cancer. SMRT and N-CoR are two closely-related transcriptional corepressors that mediate transcriptional repression by ER and are required for tamoxifen-mediated anti-proliferative activity. We hypothesize that decreased expression of SMRT or N-CoR contributes to tamoxifen-resistant breast cancer. We are interested in elucidating the mechanisms underlying stability control of the transcriptional corepressor SMRT in breast cancer.
  • 3. Investigating the function and regulation of promyelocytic leukemia protein (PML).
    PML is a tumor suppressor protein that control many cellular processes including apoptosis, cell proliferation, senescence, and transcription. PML is subjected to several post-translational modifications such as phosphorylation, sumoylation, acetylation, ubiquitination, and isgylation. We are interested in the following questions:
    • How post-translational modifications regulate PML function?
    • How the post-translational modifications of PML cross-talk with each other?
    • How PML target genes mediate its cellular function?

Selected References

  • Kristopher J Stanya and Hung-Ying Kao.
    “New insights into the functions and regulation of the transcriptional corepressors SMRT and N-CoR” (Invited Review)
    Cell Division (2009) (in press).
  • Kris Stanya, Yu Liu, Anthony Means, and Hung-Ying Kao
    “Cdk2 and Pin1 are critical for ErbB2- mediated SMRT destabilization”
    J. Cell Biol. Oct 6:183(1): 49-63 (2008) (Highlight in Trends Biochem Sci. 2009 Mar 6).
  • Chengzhuo Gao, Chun-Chen Ho, Erin Reineke, Minh Lam, Xiwen Cheng, Kris Stanya, Yu Liu, Sharmistha Chakraborty, Hsiu-Ming Shih, Hung-Ying Kao.
    “Histone deacetylase 7 promotes PML sumoylation and is essential for PML nuclear body (NB) formation.”
    Mol Cell Biol. Sep 28(18):5658-67 (2008).
  • Chengzhuo Gao, Xiwen Cheng, Minh Lam, Yu Liu1, Qing Liu, Kun-Sang Chang, and Hung-Ying Kao.
    “Signal-dependent regulation of transcription by histone deacetylase 7 (HDAC7) involves recruitment to PML nuclear bodies.”
    2008, Mol Biol Cell. Jul 19(7):3020-7 (2008).
  • Erin L. Reineke, Minh Lam, Qing Liu, Yu Liu, Kristopher J. Stanya, Kun-Sang Chang, Anthony R. Means and Hung-Ying Kao.
    “Degradation of the tumor suppressor PML by Pin1 contributes to the cancer phenotype of breast cancer MDA-MB-231 cells.”
    Mol Cell Biol. Feb 28(3):997-1006 (2008).

 

Hung-Ying Kao Faculty's publications at pubmed