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Structure, regulation and dynamics of small G proteins and their interactions with membranes and effector proteins

Department of Biochemistry

Applications accepted all year round Awaiting Funding Decision/Possible External Funding

About the Project

Our lab are interested in cell signalling via small G proteins of the Ras superfamily. We use a range of biochemical, biophysical and structural approaches to understand these fascinating proteins, which are involved in multiple cellular processes and are often deregulated in diseases such as cancer. Current projects in the lab include: using NMR to study the structures and dynamics of Rho family small G proteins and their cancer-associated mutants; development of stapled peptides to inhibit small G protein-effector interactions; structural investigation of the interactions between small G proteins and membranes; interactions between effector proteins and membranes and the consequences for G protein binding. Projects available depend on the interest and expertise of the applicant, but all are in the general topic of understanding the molecular details of small G proteins, their interactions with other proteins and with lipids, their deregulation in cancer and their inhibition.

See for more information about our work and publications.

Applications should be sent to Helen Mott (), including a CV detailing academic achievements so far, a motivational statement and the names and contact details of two referees.

Funding Notes

Funding can be obtained via Cambridge MRC or BBSRC DTPs, through Departmental AstraZeneca Studentships or via various Cambridge Scholarships including those for overseas students.


K.V. Rajasekar, L.J. Campbell, D. Nietlispach, D. Owen & H.R. Mott (2013) The structure of the RLIP76 (RalBP1) RhoGAP domain-Ral binding domain dyad: fixed position of the domains leads to dual engagement of small G proteins at the membrane. Structure 21 2131-2142.

C. L. Hutchinson, P.N. Lowe, S.H. McLaughlin, H.R. Mott & 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

L. J Campbell, M. Peppa, M.D. Crabtree, A. Shafiq, N.F. McGough, H.R. Mott & D. Owen (2015) Thermodynamic mapping of effector protein interfaces with RalA and RalB. Biochemistry. 54 1380-1389

H.R. Mott & D. Owen (2015) Structures of Ras superfamily effector complexes: What have we learnt in two decades? Crit Rev Biochem Mol Biol. 50 85-133.

J.R. Watson, H.M. Fox, D. Nietlispach, J.L. Gallop, D. Owen D & H.R. Mott (2016) Investigation of the interaction between Cdc42 and its effector TOCA1: handover of Cdc42 to the actin regulator N-WASP is facilitated by differential binding affintiies. J. Biol. Chem. 291 13875-13890.

J.C. Thomas, J.M. Cooper, N.S. Clayton, C. Wang, M.A. White, C. Abell, D. Owen & H.R. Mott (2016) Inihibition of Ral GTPases using a stapled peptide approach. J. Biol. Chem. 291 18310-18325.

H.R Mott & D. Owen (2018) Bioblockades join the assault on small G protein signalling. (2019) Semin Cancer Biol 54 149-161

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