User:Joshua S. Waitzman
- 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, kinesin-5 and other mitotic motor proteins are promising drug targets for cancer therapy, and ispinesib, a specific inhibitor of kinesin-5, is in Phase II FDA trials for non-small cell lung cancer and glioblastoma multiforme.
Kinesin-5 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 kinesin-5. Our group uses Electron Paramagnetic Resonance (EPR) spectroscopy to monitor the freedom of movement of different parts of the kinesin-5 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 kinesin-5 and may be able to guide future drug discovery efforts.
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