Staff Directory

Last Updated

09/10/2017

Email
Telephone
01522 88 6995
Post
University of Lincoln
Brayford Pool
Lincoln
Lincolnshire
LN6 7TS
United Kingdom

About Stefan Millson

I joined the University of Lincoln in 2014, and I am a Senior Lecture in the School of Life Sciences. Before coming to Lincoln I was a postdoctoral researcher at the University of Sheffield, University College London and the holder of a Bogue fellowship at the Howard Hughes Medical Institute. The main focus of my research has been molecular genetic analysis of Heat Shock Protein 90 (Hsp90), a promiscuous molecular chaperone that is currently a promising cancer drug target since it is needed for the activation of many of the proteins that drive cancer progression. I setup the UK’s first high throughput yeast two-hybrid protein interaction screening facility (Millson et al., 2003) and then used this to perform the first genomic yeast two hybrid screen for Hsp90 interactions, based on identifying the subset of interactions that are reinforced by a mutation that arrest the Hsp90 chaperone cycle (Millson et al., 2005). I then went on to study whether Hsp90-dependent processes are affected by placing different isoforms of Hsp90 in yeast cells (Millson et al., 2007), as well as the different ligand binding discriminations of Hsp90 client proteins (Millson et al., 2008). Subsequently I initiated a project designed to see how readily drug resistance could arise by mutation to very highly conserved drug binding site on Hsp90 – acquired drug resistance being such a major problem in chemotherapy treatment. It focussed on the Hsp90 proteins of microbes that produce the Hsp90-targetting antibiotics radicicol and geldanamycin, since we suspected that these might have evolved a natural resistance to cancer drugs designed on the basis of the interactions made by these antibiotics within the ADP/ATP binding site of Hsp90(Prodromou et al., 2009; Millson et al., 2010; Millson et al., 2011). My latest research (Millson et al., 2014) has addressed the TORC1 regulation of heat shock transcription factor (Hsf1), specifically whether rapamycin - selective TORC1 inhibitor approved for certain treatments – is capable of counteracting the Hsf1 activation that occurs upon inhibition of Hsp90. This Hsf1 activation, causing an induction of anti-apoptotic (“prosurvival”) heat shock proteins, often compromises the effectiveness of the Hsp90 inhibitor drugs in cancer treatment. I am also involved in collaborative research on Hsp90 system co-chaperones and on the myosin folding chaperone UNC45 (Gomez-Escalante, Piper, and Millson, 2017). https://www.facebook.com/MillsonLab/

Department Responsibilities

Postgraduate research tutor for Life Sciences. Module lead of Introduction to Clinical Biochemistry (BMS2013M).

Subject Specialism

Use of yeast as a model system to study molecular chaperone “drivers” of cancer.

Qualifications

  • PhD. Molecular Genetics — University of Greenwich, 2001
  • MSc. Molecular Biology — University of Greenwich, 1998
  • BSc (Hons). Biochemistry — Liverpool John Moores University, 1994

Orcid ID

0000-0001-5989-5759

Research Interests

  • Cancer research

  • Molecular Genetics

  • Moleular chaperones

  • Protein folding

  • Yeast

Research in the Lincoln Repository


Professional Affiliations

  • Higher Education Academy — Fellow
  • Institute of Biomedical Sciences — Fellow