Dr Sarah Coleman
Lecturer in biochemistry
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I read for a BSc (Hons) (1989) in Biochemistry at University of Essex; then for a PhD (1996) in Biochemistry at the School of Pharmacy, University of London under Prof. F. Anne Stephenson. There I examined the pharmacological and biochemical properties of NMDA receptors, a sub-family of ionotropic glutamate receptors. The title of my thesis being NMDA receptors: A Biochemical Characterization. Following this I had a brief stint at Imperial College, London examining potassium channels combinations in the brain.
I moved to Helsinki, Finland and entered the Department of Biosciences, University of Helsinki. Where I joined the Glutamate Receptor group of Professor Kari Keinänen examining AMPA receptors (another sub-family of the ionotropic glutamate receptors) their biogenesis, assembly and trafficking. In 2010 I became a Docent in Biochemistry and a University Researcher at the University of Helsinki.
In November 2015 I joined the Department of Life Science, University of Westminster as a lecturer in Biochemistry.
I am a member of The Biochemical Society (UK), British Neuroscience Association and The Society for Neuroscience (USA).
Module leader for: Level 4 Biochemistry 4BICH001W
Teaching on: 4BICH003W Science History and Philosophy and Practice; 6BICH002W Proteins and Enzymes; 6BIOL002W Advanced Cell Biology
Involved and teaching on with the University cross discipline elective (MAD and FST) Art / Science Collaboration 5WSEL001W
Involved with the University of Westminster iGEM team 2017
My research is focused on the assembly and molecular interactions of the ionotropic glutamate receptors, especially the AMPA receptor subtype and their associated proteins. AMPA receptors are tetrameric glutamate-gated cation channels and are the primary mediators of fast excitatory neurotransmission. They are fundamental for normal synaptic physiology and memory formation; they are also involved in a number of common neurological disorders, for example; intellectual disability, autism spectrum disorders, Alzheimer’s disease and schizophrenia. The receptors are composed from homologous subunits, GluA1 to A4, (generated from genes Gria1-4).
I have focused on the inherent logic of AMPA receptor assembly and trafficking; the ability of AMPA receptor subunits to associate with each other and to make a correctly localized and functional receptor in the absence of external factors, which may normally be present (in the neuron). My research has centred upon the biogenesis of AMPA receptors, i.e. from polypepetide production in the endoplasmic reticulum (ER), their assembly (via dimers, then as tetramers) through to the ER exit of the correctly folded and assembled receptors (early trafficking). Thus, the vital role of the extracellular ligand-binding domain in AMPA receptor quality control processes was demonstrated in a series of studies. Currently, I am examining the difference in trafficking behaviour of the native GluA2 vs GluA3, also including the stability and aggregation phenotypes of the respective homomeric receptors.