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Characterising a Novel Interaction between Rap1b and Rhea sheds light on new Mechanisms for Focal Adhesion Assembly

Castle, W. M. (2016) Characterising a Novel Interaction between Rap1b and Rhea sheds light on new Mechanisms for Focal Adhesion Assembly. Master of Science by Research (MScRes) thesis, University of Kent,. (KAR id:57858)

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For the first time, we reveal a direct interaction between Rap1b and the fly homolog of talin, Rhea. Using a combination of biochemical and biophysical techniques, the Rap1 binding site on Rhea has been successfully mapped. Additionally, we reveal that an acidic-to-basic K17E substitution, on Rhea, completely abolishes Rap1 binding. Our collaborators have shown that this mutation results in non-viable embryos and our data links the Rap1:Rhea interaction to this lethal phenotype. The implications of our findings support currently proposed mechanisms of RIAM-independent integrin activation, that would challenge our understanding of focal adhesion formation.

Furthermore, we propose a double-dependent Rap1 integrin-activation pathway, involving Rap1 directly interacting with the FERM domain, alongside the known Rap1-dependent recruitment of talin.

Together this work confirms a direct interaction between Rhea and Rap1 whilst providing biochemical validation for the lethal phenotypes observed in mutant flies. It also provides further insight into new mechanisms of focal adhesion formation and integrin activation.

Item Type: Thesis (Master of Science by Research (MScRes))
Thesis advisor: Goult, Benjamin T
Subjects: Q Science
Divisions: Divisions > Division of Natural Sciences > School of Biosciences
Depositing User: Users 1 not found.
Date Deposited: 12 Oct 2016 11:00 UTC
Last Modified: 20 May 2021 13:31 UTC
Resource URI: (The current URI for this page, for reference purposes)
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