Postdoctoral Fellow - Cryo-EM/X-ray crystallography

Investigating the structural basis linking HIV-1/AIDS to cancer using cryo-EM or X-ray crystallography

A postdoctoral fellowship is available to study the molecular basis of how HIV and other virus-encoded proteins hijack the centrosome duplication machinery and induce aneuploidy that can lead to carcinogenesis. The primary focus will be on determining the X-ray crystal structures for the complexes that we have isolated from our recent studies. The ultimate goal of this research is to determine the etiology of centrosome abnormality–associated cancers or other human disorders and to devise novel strategies to tackle them. Related to this project, we are also taking biochemical and cell biological approaches, including super-resolution imaging, single molecule tracking, and in vitro reconstitution to delineate the mechanism of governing Polo-like kinase 4 and 1 (Plk4/Plk1)’s functionality on the centrosomal architecture, the deregulation of which can lead to the development of many human diseases, including cancers. For additional information. please visit https://ccr.cancer.gov/staff-directory/kyung-s-lee.

Recent representative papers:

1. Discovery of a centrosomal complex linking HIV-1 infection to oncogenesis (under review).
2. Allopole, the first allosteric inhibitor targeting polo-like kinase 1 polo-box domain (under revision for PNAS, USA).
3. Ahn, J.I., et al., 2023. Architectural basis for cylindrical self-assembly governing Plk4-mediated centriole duplication in human cells. Commun. Biol. (in press).
4. Park, J.E., et al., 2023. Structural optimization and anticancer activity of inhibitors of polo-box domain (PBD) of polo-like kinase 1 (Plk1) and their prodrugs. ACS Pharma Transl Sci. 6:422.
5. Kim, T.-S., et al., 2019. Molecular architecture of a cylindrical self-assembly at human centrosomes. Nat. Comm. 10: 1151. Featured article (Editors’ Highlights).
6. Park, J.-E., et al., 2019. Phase separation of polo-like kinase 4 by autoactivation and clustering drives centriole biogenesis. Nat. Comm. 10: 4959.
7. Wei, Z., et al., 2020. Requirement of the Cep57-Cep63 interaction for proper Cep152 recruitment and centriole duplication. Mol. Cell. Biol. 40:e00535. Featured article (Cover art)
8. Ahn, J. I., et al., 2020. Phase separation and versatile capacity of pericentriolar scaffold proteins drive the formation of higher-order self-assemblies at human centrosomes. Cell Cycle. Nov 18:1-21.
9. Lee, K. S., et al., 2020. A self-assembled cylindrical platform for Plk4-induced centriole biogenesis. Open Biol. 10:200102 (Review). Featured article (Cover art)

Fellows who have expertise in the field of cryo-EM or X-ray crystallography with a keen interest in learning about the organization and function of the centrosome and their relevance to pathophysiological disorders 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 and have achieved the degree less than 3 years ago.

The NIH is dedicated to building a community in its training and employment programs and encourages the application and nomination of qualified women, minorities, and individuals with disabilities. Selection for this position will be based solely on merit, with no discrimination for non-merit reasons such as race, color, religion, gender, sexual orientation, national origin, political affiliation, marital status, disability, age, or membership or non-membership in an employee organization. The NIH encourages the application and nomination of qualified women, minorities, and individuals with disabilities.

This position is subject to a background investigation.