ArticleFEBS letters2018
Chlamydial virulence factor TarP mimics talin to disrupt the talin-vinculin complex.
Article in FEBS letters, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- Talin mechanosensitivity is modulated by a direct interaction with cyclin-dependent kinase-1.The Journal of biological chemistry · 2021Article
- Article
- Got mutants? How advances in chlamydial genetics have furthered the study of effector proteins.Pathogens and disease · 2021Review
- Manipulation of Focal Adhesion Signaling by Pathogenic Microbes.International journal of molecular sciences · 2021Review
- Increased talin-vinculin spatial proximities in livers in response to spotted fever group rickettsial and Ebola virus infections.Laboratory investigation; a journal of technical methods and pathology · 2020Article
- ELM-the eukaryotic linear motif resource in 2020.Nucleic acids research · 2020Article
- Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Vinculin is a central component of mechanosensitive adhesive complexes that form between cells and the extracellular matrix. A myriad of infectious agents mimic vinculin binding sites (VBS), enabling them to hijack the adhesion machinery and facilitate cellular entry. Here, we report the structural and biochemical characterisation of VBS from the chlamydial virulence factor TarP. Whilst the affinities of isolated VBS peptides from TarP and talin for vinculin are similar, their behaviour in larger fragments is markedly different. In talin, VBS are cryptic and require mechanical activation to bind vinculin, whereas the TarP VBS are located in disordered regions, and so are constitutively active. We demonstrate that the TarP VBS can uncouple talin:vinculin complexes, which may lead to adhesion destabilisation.
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Registered trials
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