User:Joshua S. Waitzman
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Revision as of 12:24, 9 July 2010
- Joshua S. Waitzman
- Ward 8-321
- Department of Cell and Molecular Biology
- Feinberg School of Medicine, Northwestern University
- Chicago, IL, USA 60611
- Email me through OpenWetWare
I'm an MD/PhD student working in the Rice Lab at Northwestern
- 2007, Sc.B. with Honors in Biophysics, magna cum laude, Brown University
In order to divide and proliferate, a single cell must distribute its chromsomes equally to daughter cells by establishing a microtubule-based spindle. Kinesin-5 is a microtubule motor protein that plays an essential role in aligning this spindle structure. As a hallmark of cancer cells is their increased ability to divide, Eg5 and other mitotic motor proteins are promising drug targets for cancer therapy, and ispinesib, a specific inhibitor of Eg5, is in Phase II FDA trials for non-small cell lung cancer and glioblastoma multiforme.
Eg5 is believed to be regulated by phosphorylation by both M-Cdk and Wee1, kinases known to play roles in the cell cycle. However, the structural mechanisms of this phospho-regulation are unknown. My work uses structural biology and biochemistry approaches to determine the phosphorylation-dependent changes in Eg5. Our group uses Electron Paramagnetic Resonance (EPR) spectroscopy to monitor the freedom of movement of different parts of the Eg5 protein, as well as kinetic measurements of the protein's activity. By combining these approaches, we hope to clarify the relationships between structure and activity in Eg5 and may be able to guide future drug discovery efforts.
- Duch J, Waitzman JS, and Amaral LA. . pmid:20585387.
- Bauer JH, Chang C, Morris SN, Hozier S, Andersen S, Waitzman JS, and Helfand SL. . pmid:17686972.