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Xiaoqi Liu

Biochemistry 

  • Associate Professor of Biochem/Cancer Rsr
765.496.3764
765.494.7897
HANS Room 233C

Lab Members

Area of Expertise: Roles of Polo-like kinase 1 and its interacting proteins in cell proliferation and carcinogenesis

Current therapeutic strategies for cancer patients have shown only moderate success in reducing incidence and mortality rates and improving survival, thus a new class of more specific treatments for various cancers is greatly needed. A major goal in cancer research is to understand the molecular events that are associated with this disease to aid in the development of such novel therapies. The long-term goal of my research program is to understand the molecular mechanisms that cause cancer and to use this information to provide new avenues for cancer therapy. My work focuses on an enzyme known as Polo-like kinase 1 (Plk1), which plays a central role in controlling cell division and is known to exist at abnormally high levels in many types of human cancers. Compounds that inhibit Plk1 are currently viewed as promising new anti-cancer drugs. To fully exploit Plk1 as a potential anticancer drug target, it is essential to fully understand its regulation and function, particularly in the context of the cancer cell. We have made a series of contributions to understanding both Plk1 regulation and its function and the lab is in a position to make crucial contributions in understanding how Plk1 can be exploited as a target for drugs to treat cancer and other important human diseases. The lab is currently using a combination of biochemistry, cell biology and mouse genetics to dissect the roles of Plk1 in initiation, progression and metastasis of prostate and pancreatic cancer.

Awards & Honors

(2012) Seed for Success Award. Purdue University.

Selected Publications

Hou, X., Zhiguo, L., Huang, W., Li, J., Staiger, C., Kuang, S., . . . Liu, X. (2013). Plk1-dependent microtubule dynamics promotes androgen receptor signaling in prostate cancer. The Prostate, 73, 1352-1363. Retrieved from http://onlinelibrary.wiley.com/doi/10.1002/pros.22683/abstract;jsessionid=D4E8C8B48AE9E811EAB8EFC7BF227514.d03t01

Song, B., Liu, X. S., Rice, S. J., Kuang, S., Elzey, B. D., Konieczny, S. F., . . . Liu, X. (2013). Plk1 phosphorylation of Orc2 and Hbo1 contributes to gemcitabine resistance in pancreatic cancer. Mol. Cancer Ther., 12, 58-68. Retrieved from http://mct.aacrjournals.org/content/12/1/58.long

Liu, X. S., Song, B., Tang, J., Liu, W., Kuang, S., & Liu, X. (2012). Plk1 phosphorylates Sgt1 at the kinetochores to promote timely kinetochore-microtubule attachment. Mol. Cell. Biol., 32, 4053-4067. Retrieved from http://mcb.asm.org/content/32/19/4053.full.pdf+html

Luo, J., & Liu, X. (2012). Polo-like kinase 1, on the rise from cell cycle regulation to prostate cancer development. Protein Cell, 3, 182-197.

Song, B., Liu, X. S., Davis, K., & Liu, X. (2011). Plk1 Phosphorylation of Orc2 Promotes DNA Replication under Conditions of Stress. Mol. Cell Biol., 31, 4844-4856. Retrieved from http://mcb.asm.org/content/31/23/4844.full.pdf+html

Liu, X. S., Song, B., Elzey, B. D., Ratliff, T. L., Konieczny, S. F., Cheng, L., . . . Liu, X. (2011). Polo-like kinase 1 facilitates loss of Pten tumor suppressor-induced prostate cancer formation. J. Biol. Chem., 286, 35795-35800. Retrieved from http://www.jbc.org/content/286/41/35795.full.pdf+html

Song, B., Davis, K., Liu, X. S., Lee, H. G., Smith, M., & Liu, X. (2011). Inhibition of Polo-like kinase 1 reduces beta-amyloid-induced neuronal cell death in Alzheimer's disease. Aging, 3, 846-851. Retrieved from http://www.impactaging.com/papers/v3/n9/pdf/100382.pdf

Li, H., Liu, X. S., Yang, X., Wang, Y., Wang, Y.., Turner, J. R., & Liu, X. (2010). Phosphorylation of CLIP-170 by Plk1 and CK2 promotes timely formation of kinetochore-microtubule attachments. EMBO J., 29, 2953-2965. Retrieved from http://www.nature.com/emboj/journal/v29/n17/full/emboj2010174a.html

Li, H., Liu, X. S., Yang, X., Song, B., Wang, Y., & Liu, X. (2010). Polo-like kinase 1 phosphorylation of p150Glued facilitates nuclear envelope breakdown during prophase. Proc. Natl. Acad. Sci. USA, 107, 14633-14638. Retrieved from http://www.pnas.org/content/107/33/14633.long

Liu, X. S., Li, H., Song, B., & Liu, X. (2010). Polo-like kinase 1 phosphorylation of G2 and S-phase-expressed 1 protein is essential for p53 inactivation during G2 checkpoint recovery. EMBO Rep., 11, 626-632. Retrieved from http://www.nature.com/embor/journal/v11/n8/pdf/embor201090.pdf