A postdoctoral position is available to study the function of mammalian polo-like kinases in the regulation of various biochemical and cellular events, including but not limited to centriole duplication, mitotic progression, and tumorigenesis.
Applicants should be a Ph.D. or M.D. with less than 3 years of postdoctoral experience. Expertise in biochemistry, cancer and stem cell biology is preferred. Visit https://ccrod.cancer.gov/confluence/display/CCRKLEE/Home for additional information.
To Apply:
Send CV and three references to Dr. Kyung Lee (kyunglee@mail.nih.gov).
Selected Publications:
Kang, Y.-H., et al. 2006. Self-regulated Plk1 recruitment to kinetochores by the Plk1-PBIP1 interaction is critical for proper chromosome segregation. Mol. Cell 24:409-422.
Soung NK, et al. 2009. Plk1-dependent and -independent roles of an ODF2 splice variant, hCenexin1, at the centrosome of somatic cells. Dev. Cell 16: 539-550.
Park JE, et al. 2009. Direct quantification of polo-like kinase 1 activity in cells and tissues using a highly sensitive and specific ELISA assay. PNAS USA. 106:1725-1730.
Yun SM, et al. 2009. Structural and functional analyses of minimal phosphopeptides targeting the polo-box domain of polo-like kinase 1. Nat. Str. & Mol. Biol. 16:876-882.
Park, J. -E., et al. 2011. Feed-forward mechanism of converting biochemical cooperativity to mitotic processes at the kinetochore plate. PNAS USA. 108:8200-5.
Johmura Y, et al. 2011. Regulation of microtubule-based microtubule nucleation by mammalian polo-like kinase 1. PNAS USA. 108:11446-11451.
Liu F, et al. 2011. Serendipitous alkylation of a Plk1 ligand uncovers a new binding channel. Nat. Chem. Biol. 7:595-601.
Lee KH, et al. 2012. Identification of a novel Wnt5a-CK1ε-Dvl2-Plk1-mediated primary cilia disassembly pathway. EMBO J. 31:3104-17.
This position is subject to a background investigation. The NIH is dedicated to building a diverse community in its training and employment programs.
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