Vaughan, Cara - Birkbeck, University of London - Department of Biological Sciences

研究领域

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 assembly 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 yeast Saccharomyces 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. Techniques 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.

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Mollapour M, Tsutsumi S, Truman AW, Xu W, Vaughan CK, Beebe K, Konstantinova A, Vourganti S, Panaretou B, Piper PW, Trepel JB, Prodromou C, Pearl LH, Neckers L. Threonine 22 phosphorylation attentuate Hsp90 interaction with cochaperones and affects its chaperone activity. Mol Cell. 2011 Mar 18;41(6):672-81. Vaughan CK, Neckers L, Piper PW. Understanding of the Hsp90 molecular chaperone reaches new heights. Nat Struct Mol Biol. 2010 Dec;17(12):1400-4. Vaughan CK, Piper PW, Pearl LH, Prodromou C. A common conformationally couple ATPase mechanism for yeast and human cytoplasmic Hsp90s. FEBS J. 2009 Jan 276 (1):199-209. Vaughan CK, Mollapour M, Smith JR, Truman A, Hu B, Good VM, Panaretou B, Neckers L, Clarke PA, Workman P, Piper PW, Prodromou C, Pearl LH. Hsp90-dependent activation of protein kinases is regulated by chaperone-targeted dephosphorylation of Cdc37. Mol Cell. 2008 Sep 26;31(6):886-95.