.

Dr Alice Rothnie

Dr Alice Rothnie
Dr Alice Rothnie

Lecturer in Cell Biology/Biochemistry

Research Group

Molecular Biomedical Research

Research Centre

Aston Research Centre for Healthy Ageing (ARCHA)  

Profile

I joined Aston School of Life & Health Sciences in Jan 2009, having spent the previous two years as a postdoctoral researcher in Structural Biology at Warwick University, working with Dr. Corinne Smith on the mechanism of clathrin cage disassembly by the chaperone Hsc70.

Prior to this I held a postdoctoral fellowship at the Cancer Research Institute, Queen’s University, Kinston ON, Canada, working with Prof. Susan Cole on the interaction of MRP1 (multidrug resistance protein 1) with GSH.

I completed my PhD in the lab of Dr. Richard Callaghan at the Nuffield Dept. Clinical Lab. Sciences, John Radcliffe Hospital, Oxford, on the topographical changes of TM6 of P-glycoprotein.

Qualifications & Education

  • DPhil, in Biochemistry. Nuffield Dept. Clinical Lab. Sciences, University of Oxford. 2000-2004
  • MBiochem honours (2.1), in Biochemistry. Brasenose College, University of Oxford. 1996-2000

Employment

  • Jan 2010 – present: Lecturer in Cell Biology/Biochemistry. Aston University, Birmingham, UK.
  • Sept 2007 – Dec 2009: Post-doctoral researcher, Dept. Biological Sciences, Warwick University, Coventry, UK.
  • May 2004 – Aug 2007: Post-doctoral fellow, Cancer Research Institute, Queen’s University, Kingston ON, Canada. Recipient of a CIHR (Canadian Institutes Health Research) fellowship

Research interests

My research interests lie in elucidating the mechanistic, functional details of proteins that do important jobs in the cell, both in health and disease. To date these have included membrane transporter proteins of the ABC superfamily (ATP Binding Casette) involved in drug resistance in cancer, and the chaperone proteins involved in removing the clathrin coat from endocytosed vesicles, both of which use ATP hydrolysis to drive their function, and are closely associated with cell membranes.

My approach involves the overexpression and purification of the proteins, and subsequently putting all the parts back together to form an in vitro model system in order to study the function of these complex proteins. I use a wide range of biochemical functional assays and biophysical techniques to examine the mechanism, breaking it down into its constituent steps.

The type of questions I ask include; How does a protein recognise its particular substrate(s)? What effect does substrate binding have on the conformation of the protein? How is function coupled to ATP hydrolysis? How exactly does a protein carry out its job & what is the order of events that occur? How do disease causing mutations affect the function? Does the protein require interaction with other proteins to function? How is the process regulated? 

In the future I plan to use biochemical and biophysical methods to continue examining the mechanism of clathrin cage disassembly in more detail, and to study other members of the ABC family of transporters involved in human disease.

Membership of Professional Bodies

  • Biochemical Society
  • The Protein Society
  • Molecular Chaperone Club
  • Midlands Biophysics Network

 Publications