Andrew M Fry

Director of Research, College of Medicine, Biological Sciences and PsychologyAndrew Fry

Contact details

Tel: 0116 229 7069


Personal details

  • 1985-1989 Scholarship at St. Peter's College, University of Oxford. BA (Hons) 1st class in Biochemistry, St. Peter's College, University of Oxford. Dissertation in Fission yeast cell cycle control with Professor Paul Nurse
  • 1989-1993 Research project carried out in the ICRF Molecular Oncology Laboratory at the Institute of Molecular Medicine, John Radcliffe Hospital, Oxford.  D. Phil. Thesis: Phosphorylation of the human topoisomerase II protein, supervised by Dr. Ian Hickson and Professor Adrian Harris.
  • 1993-1995 Royal Society Postdoctoral Fellow at the Swiss Institute for Experimental Cancer Research (ISREC), Lausanne, Switzerland.
  • 1995-1998 Maitre Assistant at the University of Geneva, Switzerland.
  • 1999-2005 Lecturer, Department of Biochemistry, University of Leicester
  • 2000-2005 Lister Institute Research Fellow, Department of Biochemistry, University of Leicester
  • 2005-2008 Reader, Department of Biochemistry, University of Leicester
  • 2008 Appointed to Personal Chair, Department of Biochemistry, University of Leicester
  • 2010-present Deputy Head of Department of Biochemistry
  • 2012-2014 Head of Core Biotechnology Services
  • 2014-present College Director of Research


Coxon CR, Wong C, Bayliss R, Boxall K, Carr KH, Fry AM, Hardcastle IR, Matheson CJ, Newell DR, Sivaprakasam M, Thomas H, Yoeh S, Wang LZ, Grifin RJ, Golding BT, Cano C (2016) Structure-guided design of purine-based probes for selective Nek2 inhibition.Oncotarget (in press)

Bayliss R, Choi J, Fennell DA, Fry AM and Richards M (2016) Molecular mechanisms that underpin EML4-ALK driven cancers and their response to targeted drugs. Cell and Molecular Life Sciences 73, 1209-1224.

Fry AM, O’Regan L, Montgomery J, Adib R and Bayliss R (2016) EML proteins in microtubule regulation and human disease.Biochemical Society Transactions (in press).

Mitcheson DF, Bottrill A, Carr K, Coxon, CR, Cano, C, Golding BT, Griffin RJ, Fry AM, Doerig C, Bayliss R, Tobin A (2016) A new tool for chemical genetic investigation of Plasmodium falciparum PfNek-2 NIMA-related kinase. Malaria J. 15, 535.

Richards MW, O’Regan L, Roth D, Montgomery JM, Straube A, *Fry AM, *Bayliss R (2015) Microtubule association of EML proteins and the EML4-ALK variant 3 oncoprotein requires an N-terminal trimerization domain. Biochemical Journal 467, 529-536. *Joint corresponding authors.

O’Regan L, Sampson J, Richards MW, Knebel A, Roth D, Hood FE, Straube A, Royle SJ, Bayliss R,  Fry AM (2015) Hsp72 is targeted to the mitotic spindle by Nek6 kinase to promote K-fibre assembly and mitotic progression. Journal of Cell Biology 209, 349-358.[Article highlighted In This Issue].

Prosser SL, Sahota NK, Pelletier L, Morrison CG, Fry AM (2015) Nek5 promotes centrosome integrity in interphase and loss of centrosome cohesion in mitosis. Journal of Cell Biology 209, 339-348.

Fry AM (2015) Solving the centriole disengagement puzzle. Nature Cell Biology 17, 3-5.

Prosser SL, O’Regan L and Fry AM (2015) New insights into the mechanisms of mitotic spindle assembly by NEK kinases. Molecular and Cellular Oncology 3, e1062952.

Prosser SL and Fry AM (2015) NEK5: a new regulator of centrosome integrity. Oncotarget 6, 24594-24595.

O’Regan L, Sampson J and Fry AM (2015) Hsp70 proteins in mitotic spindle assembly. Oncotarget 6, 32293-32294.

Rogerson DT, Sachdeva A, Wang K, Haq T, Kazlauskaite A, Hancock SM, Huguenin-Dezot N, Muqit MMK, Fry AM, Bayliss R, Chin JW (2015) Efficient genetic encoding of phosphoserine and its nonhydrolyzable analog. Nature Chemical Biology 11, 496-503.

Sabir SR, Sahota NK, Jones GDD, Fry AM (2015) Loss of Nek11 prevents G2/M arrest and promotes cell death in HCT116 colorectal cancer cells exposed to therapeutic DNA damaging agentsPLoS ONE 10, e0140975.

Haq T, Richards MW, Burgess SG, Gallego P, Yeoh S, O’Regan L, Reverter D, Roig J, Fry AM, Bayliss R (2015) Mechanistic basis of Nek7 activation through Nek9 binding and induced dimerization. Nature Communications 6, 8771.

Jamaladdin S, Kelly RDW, O’Regan L, Dovey OM, Hodson G, Millard C, Fry AM, Schwabe J, Cowley S (2014) Histone deacetylases (HDAC) 1 and 2 are essential for accurate cell division and the pluripotency of embryonic stem cells. Proc. Natl. Acad. Sci. (U.S.A.) 111, 9840-9845.

Thauvin-Robinet C, Lee JS, Lopez E, Herranz-Perez V, Franco B, Jego L, Shida T, Ye F, Pasquier L, Loget P, Gigot N, Aral B, Lopes CAM, Thevenon J, Munnich A, Vekemans M, Huet F, Fry AM, Saunier S, Riviere JB, Attie-Bitach T, Garcia-Verdugo JM, Faivre L, Megarbane A, Nachury MV (2014) The oral-facial-digital syndrome gene C2CD3 is a positive regulator of centriole elongation. Nature Genetics 46, 905-911.

Neal CP, Fry AM, Moreman C, McGregor A, Garcea G, Berry DP, Manson MM (2014) Overexpression of the Nek2 kinase in colorectal cancer correlates with beta-catenin relocalization and shortened cancer-specific survival. Journal of Surgical Oncology 110, 828-838.

Beck BB, Phillips JB, Bartram MP, Wegner J, Thoenes M, Pannes A, Sampson J, HellerR, Göbel H, Koerber F, Neugebauer A, Hedergott A, Nürnberg G, Nürnberg P, Thiele H, Altmüller J, Toliat, M.R., Staubach S, Boycott KM, Valente EM, Janecke AR, Eisenberger T, Bergmann C, Tebbe L, Wang Y, Wu Y, Fry AM, Westerfield M, Wolfrum U, Bolz HJ (2014) Mutation of POC1B in severe syndromic retinal ciliopathy. Human Mutation 35, 1153-1162.

Jerman S, Ward HH, Lee R, Lopes CAM, Fry AM, McDougall M, Wandinger-Ness A (2014) OFD1 and flotillins are integral components of a ciliary signaling protein complex organized by polycystins in renal epithelia and odontoblasts. PLoS ONE 9: e106330.

Patel JT, Bottrill A, Prosser S, Jayaraman S, Straatman KR, Fry AM, Shackleton S (2014) Mitotic phosphorylation of SUN1 loosens its connection with the nuclear lamina whilst the LINC complex remains intact. Nucleus 5, 462-473.

Hardy, T., Lee, M., Hames, R.S., Prosser, S.L., Cheary, D-M., Samant, M.D., Schultz, F., Baxter, J.E., Rhee, K. and Fry, A.M. (2014) Multisite phosphorylation of C-Nap1 releases it from Cep135 to trigger centrosome disjunction. Journal of Cell Science 127, 2493-506

Fry AM, Leaper M and Bayliss R (2014) The primary cilium: guardian of organ development and homeostasis. Organogenesis 10, 62-68.

Richards MW, Law EWP, Rennalls LP, Busacca S, O’Regan L, Straube A, Fry AM, Fennell DA, Bayliss R (2014) Crystal structure of EML1 reveals the basis for Hsp90-dependence of oncogenic EML4-ALK by disruption of an atypical b-propeller domain. Proc. Natl. Acad. Sci. (U.S.A.) 111, 5195-5200.

Mardin BR, Isokane M, Cosenza MR, Kramer A, Ellenberg J, Fry AM, Schiebel E (2013) EGF-induced centrosome separation promotes mitotic progression and cell survival. Developmental Cell 25, 229-240. [Journal Cover Image]

Fry AM (2013) Cdc20 turnover rate: a key determinant in cancer patient response to anti-mitotic therapies? Bioessays May 16. doi: 10.1002/bies.201300053

Dodson CA, Haq T, Yeoh S, Fry AM, Bayliss R (2013) The structural mechanisms that underpin mitotic kinase activation. Biochemical Society Transactions 41, 1037-1041.

Venoux, M., Tait, X., Hames, R.S. Straatman, K.R., Woodland, H.R. and Fry, A.M. (2013) Poc1A and Poc1B act together in human cells to ensure centriole integrity. Journal of Cell Science 126, 163-175.

Prosser SL, Samant MD, Morrison CE, Baxter JE, Fry AM (2012) Oscillation of APC/C activity during cell cycle arrest drives centrosome amplification. Journal of Cell Science 125, 5353-5368.

Fry AM, O’Regan L, Sabir SR, Bayliss R (2012) Cell cycle regulation by the NEK family of protein kinases. Journal of Cell Science 125, 4423-4433.Bayliss R, Fry AM, Haq T, Yeoh S (2012) On the molecular mechanisms of mitotic kinase activation. Open Biology 2, 120136.

Innocenti P, Cheung K-WJ, Solanki S, Mas-Droux C, Rowan F, Yeoh S, Boxall K, Westlake M, Pickard L, Hardy T, Baxter JE, Aherne GW, Bayliss R, Fry, AM, Hoelder S (2012) Design of potent and selective hybrid inhibitors of the mitotic kinase Nek2: SAR, structural biology and cellular activity. Journal of Medicinal Chemistry 55, 3228-3241.

Zalli D, Bayliss R, Fry AM (2012) The Nek8 protein kinase Nek8, mutated in the human cystic kidney disease nephronophthisis, is both activated and degraded during ciliogenesis. Human Molecular Genetics 21, 1155-1171.

Sahota N, Sabir S, O’Regan L, Blot J, Zalli D, Baxter J, Barone G, Fry AM (2011) NEKs, NIMA-related kinases in Encyclopedia of Signaling Molecules. Edited by S. Choi. Springer.

Croasdale R, Ivins FJ, Muskett F, Daviter T, Scott DJ, Hardy T, Smerdon SJ, Fry AM, Pfuhl M (2011) An undecided coiled-coil: the leucine zipper of Nek2 exhibits atypical conformational exchange dynamics. Journal of Biological Chemistry 286, 27537-27547.

Alexander J, Lim D, Joughin BA, Hegemann B, Hutchins JR, Ehrenberger T, Ivins F, Sessa F, Hudecz, O, Nigg EA, Fry AM, Musacchio A, Stukenberg, PT, Mechtler K, Peters J-M, Smerdon SJ, Yaffe MB (2011) Spatial exclusivity combined with positive and negative selection of phosphorylation motifs is the basis for context-dependent mitotic signaling. Science Signaling 4: ra42

Lopes CAM, Prosser S, Romio L, Merdes A, Hirst R, O’Callaghan C, Woolf A, Fry AM (2011) The oral-facial-digital syndrome type 1 protein, OFD1, interacts with PCM-1 and is required for centriolar satellite formation and basal body assembly. Journal of Cell Science 124, 600-612.

Fry AM (2011) A role for Nek6 kinase activity in preventing senescence? Cell Cycle 10, 23-2.

Mardin B, Lange C, Baxter JE, Hardy T, Scholz SR, Fry AM, Schiebel E (2010) Components of the Hippo pathway cooperate with Nek2 kinase to regulate centrosome disjunction. Nature Cell Biology 12, 1166-1176.

Hayward DG, Newbatt Y, Pickard L, Byrne E, Mao G, Burns S, Sahota NK, Workman P, Collins I, Aherne W, Fry AM (2010) Identification by high-throughput screening of viridin analogs as biochemical and cell-based inhibitors of the cell cycle-regulated Nek2 kinase. Journal of Biomolecular Screening 15, 918-927. [Cover image provided for this issue of the journal]

Fry AM, O’Regan L, Sabir SR, Bayliss R (2012) Cell cycle regulation by the NEK family of protein kinases. Journal of Cell Science 125, 4423-4433.


  • The Molecular Control of Cell Division
  • Fluorescent Microscope Imaging Facility

The goal of my research is to identify novel and important mechanisms that control human cell division with a particular focus on regulation of the microtubule cytoskeleton. My ambition is to understand how microtubules and microtubule organising centres are remodelled during progression through the cell cycle, including how primary cilia are assembled and resorbed upon entry into and exit from quiescence, and how interphase microtubule arrays are converted into a bipolar spindle upon transition into mitosis.

One specific aim of this research is to provide new insights into the complex organisation of the mammalian centrosome, while much of my work involves studying how the 11 members of the human NEK serine/threonine kinase family control these events. The overarching purpose is to answer fundamental questions about microtubule biology and cell cycle control, discover how defects in these processes contribute to human disease, including cancer, and search for new and innovative therapies that exploit these discoveries.

This image shows a human cell in the process of mitosis as it divides in two. It was taken using a fluorescence microscope and reveals the chromosomes, on which the entire human genome is encoded. The chromosomes (blue) are moved into the centre of the cell through the action of fibrous microtubules (green) and attach to the chromosomes through specialised protein structures, called kinetochores (red). This stage of mitosis is known as metaphase, following which the duplicated chromosomes will be pulled apart to opposite ends of the cell before the cell cleaves in two.

My research approach uses state-of-the-art molecular, biochemical and cell biology techniques, most notably exploiting a wide range of fixed and live cell imaging modalities, while he collaborates extensively to answer questions of basic mechanisms and medical relevance with structural biologists, biophysicists, medicinal chemists and clinical academics.

Finally, in his role as Director of Research, Professor Fry is keen to contribute to strategic developments that will create a discovery-enabling academic environment and improve training opportunities for the next generation of scientists.


This image shows a human cell in the process of mitosis as it divides in two. It was taken using a fluorescence microscope and reveals the chromosomes, on which the entire human genome is encoded.

The chromosomes (blue) are moved into the centre of the cell through the action of fibrous microtubules (green) and attach to the chromosomes through specialised protein structures, called kinetochores (red). This stage of mitosis is known as metaphase, following which the duplicated chromosomes will be pulled apart to opposite ends of the cell before the cell cleaves in two.

Fry Group members

Principal Investigator

Professor Andrew Fry

Postdoctoral Research

Laura O'Regan

Rob Turnbull

Postgraduate Students

Rozita Adib

Karolin Kroese

Josephina Sampson

Anita Singh


Technical Staff

Tara Hardy

Share this page:

Contact Details

Department of Molecular and Cell Biology

T: +44(0)116 229 7038

Map with link to google maps geotag of Henry Wellcome

Henry Wellcome Building - University of Leicester, Lancaster Rd, LE1 7HB

Postal: Henry Wellcome Building, University of Leicester, Leicester, LE1 7RH


DisabledGo logo

The University of Leicester is committed to equal access to our facilities. DisabledGo has a detailed accessibility guide for the Henry Wellcome Building.

Redfearn Lecture 2017

To Be Confirmed