Our lab are interested in protein-protein interactions in cell signaling. We focus on the Ras superfamily small G proteins, in particular the Ras and Rho family. These proteins impact on cell signaling via their interactions with an enormous number of downstream targets, known as effector proteins. We are a structural biology lab, primarily using NMR to solve structures and study the dynamics of small G proteins and their effector complexes. However, we also use a wide range of biophysical and biochemical techniques to study protein interactions and to understand the mechanisms of action of the effectors. Our work also extends into cell culture to study interactions in a more physiological setting and into design of inhibitory peptides that may provide a basis for therapeutics. We offer projects in the following broad areas: signalling pathways downstream of Ras, particularly those involving the RalA and RalB small G proteins and their downstream effectors; Rho family-effector interactions and the consequences of effector activation. For more details on some of our projects please visit the lab webpage: http://www2.bio.cam.ac.uk/~hrm28/
- Fenwick RB, Campbell LJ, Rajasekar K, Prasannan S, Nietlispach D, Camonis J, Owen D, Mott HR (2010) The RalB-RLIP76 complex reveals a novel mode of Ral-effector interaction. Structure 18 985-995.
- Hutchinson CL, Lowe PN, McLaughlin SH, Mott HR, Owen D. (2013) Differential binding of RhoA, RhoB, and RhoC to protein kinase C-related kinase (PRK) isoforms PRK1, PRK2, and PRK3: PRKs have the highest affinity for RhoB. Biochemistry 52 7999-8011
- Rajasekar KV, Campbell LJ, Nietlispach D, Owen D, Mott HR (2013) The Structure of the RLIP76 RhoGAP-Ral Binding Domain Dyad: Fixed Position of the Domains Leads to Dual Engagement of Small G Proteins at the Membrane. Structure 21 2131-2142.