Structure, regulation and dynamics of small G proteins and their interactions with membranes and effector proteins at University of Cambridge on FindAPhD.com

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Dr H Mott Applications accepted all year round Awaiting Funding Decision/Possible External Funding

Cambridge United Kingdom Biochemistry Biophysics Cancer Biology Molecular Biology Polymer Chemistry Structural Biology

Department of Biochemistry, University of Cambridge

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 https://www.bioc.cam.ac.uk/mottowen for more information about our work and publications.

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

Funding Notes

Interested students are encouraged to apply to the Cambridge Cancer Centre (View Website) which has a deadline of 15th November 2021. Other opportunities will be added as this year's deadlines are announced.

References

S.G. Chamberlain, A., Gohlke, A. Shafiq, I.J. Squires, D. Owen & H.R. Mott (2021) Calmodulin extracts the Ras family protein RalA from lipid bilayers by engagement with two membrane-targeting motifs.Proc Natl Acad Sci U S A. 118 e2104219118
J. Cornish, S.G. Chamberlain, D. Owen & H.R. Mott (2020) Intrinsically disordered proteins and membranes: a marriage of convenience for cell signalling?
Biochem Soc Trans. 2020 48 2669-2689.
H.R Mott & D. Owen (2019) Bioblockades join the assault on small G protein signalling. Semin Cancer Biol 54 149-161
J.R. Watson, H.M. Fox, D. Nietlispach, J.L. Gallop, D. Owen & 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) Inhibition of Ral GTPases using a stapled peptide approach. J. Biol. Chem. 291 18310-18325.
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.
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.