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Exploring the interactions between Vinculin and vinculin-binding site containing proteins

Paige, Thomas Joshua (2021) Exploring the interactions between Vinculin and vinculin-binding site containing proteins. Master of Science by Research (MScRes) thesis, University of Kent,. (doi:10.22024/UniKent/01.02.88510) (Access to this publication is currently restricted. You may be able to access a copy if URLs are provided) (KAR id:88510)

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Official URL:
https://doi.org/10.22024/UniKent/01.02.88510

Abstract

Focal adhesion complexes are mechanosensitive adhesion complexes that regulate keycellular processes such as cell migration and cell survival. These complexes connectthe extracellular matrix (ECM) to the Actin network through a matrix-Integrin-TalinVinculin-Actin complex. Vinculin is a linker protein that through its N-terminal headdomain (VD1) binds to cryptic vinculin binding sites (VBS) in talin, while its tail domainbinds to actin linking the actin network to the ECM. This study investigates keyinteractions between vinculin and VBS containing proteins. Proteins such as thechlamydial virulence factor TarP which hijacks vinculin to aid in bacterial internalisation,the Talin helix 50 VBS which seems unique in its ability to accommodate VD1 mutationsthat disrupt binding and lastly α-Catulin a vinculin homologue which could shareinteractions with any known vinculin binding proteins.We identified that the C.caviae Tarp VBS3 showed increased affinity for VD1 comparedto the VBS1 and Pulldown assays showed that TarP may bind VD1 in a 1:3 ratio. Wepropose that TarP binding VD1 in a 1:3 ratio alongside the differences in affinitybetween its VBS indicate the possibility of infection stage specificity between VBSs.Talin H50 appears to accommodate VD1 mutants due to of lack polar/ionic bonds,alongside smaller side chained amino acids in the interface when compared to otherVBS.Lastly, α-catulin shows conserved secondary structure with vinculin, as well as apotential interaction between α-catulin and the adhesion protein Paxillin. Indicating thatα-catulin like vinculin may bind paxillin and be recruited to focal adhesion complexes.

Item Type: Thesis (Master of Science by Research (MScRes))
Thesis advisor: Goult, Ben
DOI/Identification number: 10.22024/UniKent/01.02.88510
Uncontrolled keywords: Biochemistry, Biophysics, Mechanobiology, Structural biology
Divisions: Divisions > Division of Natural Sciences > Biosciences
SWORD Depositor: System Moodle
Depositing User: System Moodle
Date Deposited: 02 Jun 2021 16:10 UTC
Last Modified: 08 Jun 2021 08:57 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/88510 (The current URI for this page, for reference purposes)

University of Kent Author Information

Paige, Thomas Joshua.

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