School of Biosciences

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About

Dr. Christopher Mulligan joined the School of Biosciences in May 2017. Chris obtained a degree in Biochemistry from the University of York (2004). Chris performed his thesis research with Dr. Gavin Thomas at the University of York (2004-2008) and subsequently took up a postdoctoral position in the same lab (2008-2011). Here, Chris studied the structure and function of transporters involved in the uptake of virulence factors into human pathogens. Following his time in York, Chris obtained a visiting fellow position in Dr. Joseph Mindell’s lab in the Membrane Transport Biophysics Section of the National Institute of Neurological Disorders and Stroke (NINDS) at the National Institutes of Health (NIH) in Maryland, USA. During his time at NIH, Chris studied the structure and mechanism of transport protein families involved in a number of key cellular functions, including neurotransmission and metabolic regulation.

In May 2017, Chris joined the School of Biosciences as a Lecturer in Molecular Biosciences. Chris’s lab will take a multidisciplinary and collaborative approach to understanding the molecular mechanism of transporters, with an interest in transporters involved in antimicrobial resistance, bacterial virulence, nutrient uptake, and those that can be exploited in industrial biotechnology.

Twitter: @Chris_mulligan

ORCID ID: 0000-0001-5157-4651

Contact Information

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Publications

Also view these in the Kent Academic Repository

Article
Fitzgerald, G., Mulligan, C. and Mindell, J. (2017). A general method for determining secondary active transporter substrate stoichiometry. eLife [Online] 6:e21016. Available at: http://dx.doi.org/10.7554/eLife.21016.
Mulligan, C. et al. (2016). The bacterial dicarboxylate transporter VcINDY uses a two-domain elevator-type mechanism. Nature structural & molecular biology [Online] 23:256-263. Available at: http://dx.doi.org/10.1038/nsmb.3166.
Vergara-Jaque, A. et al. (2015). Family resemblances: A common fold for some dimeric ion-coupled secondary transporters. The Journal of General Physiology [Online] 146:423-434. Available at: http://dx.doi.org/10.1085/jgp.201511481.
Mulligan, C. et al. (2014). Functional characterization of a Na+-dependent dicarboxylate transporter from Vibrio cholerae. The Journal of General Physiology [Online] 143:745-759. Available at: http://dx.doi.org/10.1085/jgp.201311141.
Mulligan, C. and Mindell, J. (2013). Mechanism of transport modulation by an extracellular loop in an archaeal excitatory amino acid transporter (EAAT) homolog. Journal of Biological Chemistry [Online] 288:35266-35276. Available at: http://dx.doi.org/10.1074/jbc.M113.508408.
Mulligan, C. et al. (2012). The membrane proteins SiaQ and SiaM form an essential stoichiometric complex in the sialic acid tripartite ATP-independent periplasmic (TRAP) transporter SiaPQM (VC1777-1779) from Vibrio cholerae. Journal of Biological Chemistry [Online] 287:3598-3608. Available at: http://dx.doi.org/10.1074/jbc.M111.281030.
Mulligan, C., Fischer, M. and Thomas, G. (2010). Tripartite ATP-independent periplasmic (TRAP) transporters in bacteria and archaea. FEMS microbiology reviews [Online] 35:68-86. Available at: http://dx.doi.org/10.1111/j.1574-6976.2010.00236.x.
Mulligan, C. et al. (2009). The substrate-binding protein imposes directionality on an electrochemical sodium gradient-driven TRAP transporter. Proceedings of the National Academy of Sciences of the United States of America [Online] 106:1778-1783. Available at: http://dx.doi.org/10.1073/pnas.0809979106.
Book section
Mulligan, C. and Mindell, J. (2017). Pinning down the mechanism of transport: probing the structure and function of transporters using cysteine crosslinking and site-specific labelling. in: Ziegler, C. ed. Methods in Enzymology: A Structure-Function Toolbox for Membrane Transporter and Channels. Elsevier, pp. 165-202. Available at: https://doi.org/10.1016/bs.mie.2017.05.012.
Showing 9 of 11 total publications in KAR. [See all in KAR]
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Research Interests

Transport proteins play a major role in crucial cellular processes in all forms of life; from the uptake of nutrients and virulence factors to the extrusion of toxins (including antibiotics) in bacteria, as well as the regulation of neurotransmission and metabolism in mammals.

In humans, improper regulation and mutations in transporters are often associated with disease states like ALS, Alzheimer’s disease and epilepsy. Whereas, in bacteria, transporters contribute substantially to the virulence of human pathogens and their resistance to antibiotics, making them prime targets for new therapeutics. In addition, transporters are also key players in industrial biotechnology. Bacterial cell factories that are used to produce high value chemicals for industrial and medical purposes rely heavily on transport proteins to take up precursors and extrude the final products.

Transport proteins are highly dynamic molecular machines, most of which actively pump their substrates across the membrane fueled by an energy source; usually either ATP hydrolysis or electrochemical gradients (H+ and Na+ gradients). My lab uses a combination of biochemical, biophysical and microbiological techniques to understand the molecular mechanisms of transport proteins; how they recognise compounds, how they harness an energy source to pump compounds across the membrane, and how they move during transport. The more we understand about the mechanism of transporters, the better placed we will be to manipulate their function; either inhibiting them if they have undesirable effects, for example, antimicrobial resistance; or harnessing and enhancing their capabilities if they are useful, for example, for applications in industrial biotechnology.

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Other activities

  • Member of the Microbiology Society.
  • Member of the Biochemical Society.
  • Member of Crossing Biological Membranes Network (CBMNet), a BBSRC Network in Industrial Biotechnology and Bioenergy.
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Enquiries: Phone: +44 (0)1227 823743

School of Biosciences, University of Kent, Canterbury, Kent, CT2 7NJ

Last Updated: 18/05/2017