Investigating the structural basis linking HIV-1/AIDS to cancer
Position Description: 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.
Fellows who have an expertise in the field of 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.
To apply, please send CV and three names of references to Dr. Kyung Lee (firstname.lastname@example.org). Starts at $59,900 for fellows with 0 yr postdoc training (+ annual raise) and full health insurance
Employer Name: National Cancer Institute, NIH.
Position Location: 9000 Rockville Pike, Bethesda, MD 20892, U. S. A.
- Kim, T.-S., et al., 2019. Molecular architecture of a cylindrical self-assembly at human centrosomes. Nat. Comm. 10: 1151. Featured article (Editors’ Highlights).
- Park, J.-E., et al., 2019. Phase separation of polo-like kinase 4 by autoactivation and clustering drives centriole biogenesis. Nat. Comm. 10: 4959.
- 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)
- 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.
- 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)
Disclaimer: This position is subject to a background investigation. The NIH is dedicated to building a diverse community in its training and employment programs.