In combination with lipid phosphoinositides, the Ras superfamily of GTPases play important roles in mediating membrane trafficking processes throughout the cell. This process is controlled by the ability of Ras superfamily GTPases to cycle between a active GTP bound form and an inactive GDP bound form. This induces conformational changes in the GTPase that mediate interactions with specific protein binding partners which in turn mediate specific signalling and membrane trafficking events. 

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We are keenly interested in studying the enzymes that control the proper localization and activation of Ras superfamily GTPases in specific cellular organelles. These include Guanine Nucleotide Exchange Factors (GEFs) and GTPase activating proteins (GAPs) that control the nucleotide binding state. We have recently solved the structure of the first structurally characterised GEF for the GTPase Rab11 (Jenkins et al Nature Comms 2018). Future studies are focusing on other Rab and Arf GEF/GAP proteins, and understanding their roles in membrane trafficking and human disease. 

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Finally, we also have a keen interest in understanding how Ras superfamily GTPases recruit and activate their downstream effectors, with a particular focus on studying the PI3Ks/PI4Ks and their interactions Ras superfamily GTPases.