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Structural Studies on Focal Adhesions

Total Cost €


EC-Contrib. €






 FocAd project word cloud

Explore the words cloud of the FocAd project. It provides you a very rough idea of what is the project "FocAd" about.

fa    core    triggered    environment    cancers    membranes    systematic    sensitive    players    complexes    combination    employ    cryo    unclear    ligand    transduce    fas    light    force    learned    hierarchical    cell    integrin    techniques    cells    migration    crystallography    medically    biology    questions    polarization    tension    points    protein    macromolecular    sophisticated    regulation    lessons    detrimental    cytoskeletons    biophysical    function    implicated    spectrometry    governing    cutting    molecular    platform    observe    cytoskeleton    clarified    ultrastructural    gigantic    hybrid    networks    counteracting    survival    recombinant    developmental    stepwise    tested    focal    transferred    super    tackle    fashion    fundamental    innovative    purified    outside    ray    assembly    edge    machinery    aggressive    expertise    defects    initiating    biochemical    assemblies    reconstitutions    adhesions    regarding    emerged    leads    signaling    basis    sensing    contributes    anchoring    hence    behavior    activation    living    structural    microscopy    mass    actin    components    mechanisms    em   

Project "FocAd" data sheet

The following table provides information about the project.


Organization address
city: Munich
postcode: 80539

contact info
title: n.a.
name: n.a.
surname: n.a.
function: n.a.
email: n.a.
telephone: n.a.
fax: n.a.

 Coordinator Country Germany [DE]
 Total cost 1˙999˙998 €
 EC max contribution 1˙999˙998 € (100%)
 Programme 1. H2020-EU.1.1. (EXCELLENT SCIENCE - European Research Council (ERC))
 Code Call ERC-2016-COG
 Funding Scheme ERC-COG
 Starting year 2017
 Duration (year-month-day) from 2017-07-01   to  2022-06-30


Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 


 Project objective

Focal adhesions (FA) are gigantic protein complexes whose formation is triggered by integrin ligand activation. FAs represent (1) a sensing platform and anchoring points to the outside environment and, (2) a machinery to transduce this information by initiating signaling pathways for cell growth, survival, migration and polarization. Failure in the regulation of FA leads to developmental defects and contributes to the formation of aggressive cancers. Hence, understanding FA formation is the basis for counteracting these detrimental effects. Recently, mass spectrometry and advanced light microscopy clarified players involved in the FA assembly and implicated sophisticated regulation networks of membranes and actin cytoskeletons in the growth of FAs. However, the molecular mechanisms of FA formation and signaling still remain unclear. We propose to study the molecular mechanisms governing the growth of FA by bottom-up reconstitutions using purified recombinant protein components. We will employ a systematic and hierarchical assembly of the FA machinery on an integrin platform as well as on an actin cytoskeleton in a stepwise fashion. We will use a combination of cutting-edge techniques of hybrid structural biology (cryo-EM and X-ray crystallography), light microscopy and biochemical/biophysical approaches. Our core expertise is cryo-EM, which has emerged as the method of choice to study the molecular mechanisms of (super-)macromolecular assemblies. Furthermore, we will set up a system to observe the behavior of tension-sensitive FA components in the presence of force under cryo-EM. Finally, lessons learned from our biochemical and ultrastructural analysis will be directly transferred and tested in living cells. Using these innovative methods, we will tackle fundamental and medically relevant questions regarding the assembly and function of FAs.


year authors and title journal last update
List of publications.
2019 Dirk Dedden, Stephanie Schumacher, Charlotte F. Kelley, Martin Zacharias, Christian Biertümpfel, Reinhard Fässler, Naoko Mizuno
The Architecture of Talin1 Reveals an Autoinhibition Mechanism
published pages: 120-131.e13, ISSN: 0092-8674, DOI: 10.1016/j.cell.2019.08.034
Cell 179/1 2019-12-17

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The information about "FOCAD" are provided by the European Opendata Portal: CORDIS opendata.

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