Every heartbeat requires a large change in the level of calcium ions within cardiac cells (cardiomyocytes). This involves release of internal calcium stores caused by the opening of a channel structure known as the cardiac ryanodine receptor (RyR2), which is a large protein composed of four equal subunits. Abnormal RyR2 opening-closing is caused by genetic defects or environmental factors that can produce an irregular heartbeat (arrhythmias) and sudden death.

Research in my laboratory is focused on understanding the structure-function relationship of the RyR2 calcium release channel, as well as its regulation by accessory proteins including calsequestrin and the FK506-binding proteins. Our specific aims are twofold:  first, to elucidate the molecular mechanism(s) underlying RyR2 channel dysfunction and abnormal cardiomyocyte calcium handling in arrhythmogenic disorders. Second, to identify drug(s) that restore RyR2 protein-protein interactions and normal channel properties in order to improve intracellular calcium handling and cardiac function. We use various computational, molecular, cellular and physiological approaches, which are available in my group or provided through collaborators with established expertise. My group is supported by the British Heart Foundation (past Intermediate Fellowship and current Senior Research Fellowship).

Areas of Expertise

  • Calcium signalling
  • Excitation-contraction coupling
  • Arrhythmogenic cardiac disease


  1. & Association of cardiac myosin-binding protein-C with the ryanodine receptor channel – putative retrograde regulation?. Journal of Cell Science 131(15), jcs210443
  2. & Association of cardiac myosin-binding protein-C with the ryanodine receptor channel – putative retrograde regulation?. Journal of Cell Science 131(15), jcs210443
  3. & Calsequestrin interacts directly with the cardiac ryanodine receptor luminal domain. Journal of Cell Science, jcs.191643
  4. & Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study. Journal of Visualized Experiments(113)
  5. & Structural and functional interactions within ryanodine receptor. Biochemical Society Transactions 43(3), 377-383.

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  • PM-266 The Cardiovascular System

    Leading on from the first year Human Physiology Module (PM-139), the Cardiovascular Module will introduce and define the fundamental cellular mechanisms that regulate the physiology of healthy cardiovascular function. The Module will describe the processes that allow regular heartbeat and blood vessel function and how perturbations in the systems covered may lead to pathophysiological conditions. There will be an emphasis on experimental approaches used to study the cardiovascular mechanisms described.

  • PM-266C Y System Gardiofasgwlaidd

    Gan adeiladu ar fodiwl y flwyddyn gyntaf, Ffisioleg Ddynol (PM-139), bydd y modiwl ar y System Gardiofasgwlaidd yn cyflwyno ac yn diffinio'r mecanweithiau cellol sylfaenol sy'n rheoli ffisioleg gweithrediad system gardiofasgwlaidd iach. Bydd y modiwl yn disgrifio'r prosesau sy'n gyfrifol am guriad calon rheolaidd a gweithrediad y pibellau gwaed, a sut gall newidiadau yn y systemau dan sylw arwain at gyflyrau pathoffisiolegol. Bydd pwyslais ar y dulliau arbrofol a ddefnyddir i astudio'r mecanweithiau cardiofasgwlaidd a ddisgrifiwyd.