Studying centrosomal complexes using X-ray crystallography, NMR, EM, or biochemistry/cell biology

Bethesda, Maryland (US)
Starts at $52,900 for fellows with 0 yr postdoc training (+ anaual raise) and full health insurance
July 26 2017
Position Type
Full Time
Organization Type

Investigating the structure and function of centrosomal protein complexes using X-ray crystallography, NMR, EM, or biochemistry/cell biological approaches including single molecule super-resolution imaging

Position Description: We are mainly interested in understanding the structural basis of how various centrosomal protein complexes are generated and how these complexes work together to form a macroscale self-assembly with distinct cellular functions. Recently, we found that Polo-like kinases (Plk4 and Plk1) form high M.W. complexes with diverse binding targets. Tight regulation of the formation of these complexes appears to be critically required for the prevention of cancer development in humans. Thus, we aim to investigate the molecular mechanisms of how these complexes are formed and how they further interact with one another to generate a higher-order assembly and promote cellular processes central for cell cycle progression, proliferation and tumorigenesis.

Fellows who have an expertise in either 1) X-ray crystallography or NMR with an interest in learning various electron microscopy applications at NIH facilities or 2) classical cell biology and biochemistry with an interest in various super-resolution imaging approaches are encouraged to apply.

Applicants should have a Ph.D. (or expected to receive a Ph.D.) or M.D. equivalent at the time of joining the lab or have achieved the degree less than 3 years ago. For additional information, please click the link below.

To apply, please send CV and three names of references to Dr. Kyung Lee (

Employer Name: National Cancer Institute, NIH.

Position Location: 9000 Rockville Pike, Bethesda, MD 20892, U. S. A.


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-CK1e-Dvl2-Plk1-mediated primary cilia disassembly pathway. EMBO J. 31:3104-17.

Park, S. -Y., et al. 2014. Molecular basis for unidirectional scaffold switching of Plk4 in centriole biogenesis. Nat. Str. Mol. Biol. 21:696

Lee, K. S., T. R. Burke, J. -E. Park, J. K. Bang, E. Lee. 2015. Recent advances and new strategies in targeting Plk1 for anticancer therapy. Trends in Pharmacological Sciences. 36:858-877 (review).

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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