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- Structural & Molecular Biology
- Div of Biosciences
- Faculty of Life Sciences
The molecular chaperone Hsp90 is involved in the activation of many proteins involved in signal transduction and cell cycle pathways, making it a critical determinant of proper cellular function.
Hsp90-dependent kinetochore assemby
A recently discovered role of Hsp90 is in the assembly and/or regulation of the kinetochore. This is part of the mitotic apparatus that functions in the segregation sister chromatids to daughter cells. The kinetochore assembles on centromeric DNA forming a bridge between sister chromatids and the microtubules of the spindle pole and has the ability to maintain this connection despite the rapid polymerisation and depolymerisation of the attached microtubules. It is also the origin of the spindle assembly checkpoint that signals the anaphase-wait.
My current research focuses on the role of Hsp90 in kinetochore assembly and function, using the budding yeastSaccharomyces cerevisiae as a model organism.
Post Translational Modification of Hsp90 Cochaperones
Post translational modification of Hsp90 and its cochaperones is emerging as an important layer of regulation of Hsp90 function. I am currently interested in understanding the structural and functional consequences of phosphorylation of Hsp90 cochaperones.
The techniques we use include X-ray crystallography and single particle electron microscopy, but other biophysical and biochemical techniques are used to complement structural studies.
|1999||PhD||Doctor of Philosophy – Crystallography||University of Cambridge|
|1994||BSc Hons||Bachelor of Science (Honours) – Chemistry||University of Glasgow|