All

What are you looking for?

All
Projects
Results
Organizations

Quick search

  • Projects supported by TA ČR
  • Excellent projects
  • Projects with the highest public support
  • Current projects

Smart search

  • That is how I find a specific +word
  • That is how I leave the -word out of the results
  • “That is how I can find the whole phrase”

CAS directly interacts with vinculin to control mechanosensing and focal adhesion dynamics

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F14%3A10210779" target="_blank" >RIV/00216208:11310/14:10210779 - isvavai.cz</a>

  • Result on the web

    <a href="http://dx.doi.org/10.1007/s00018-013-1450-x" target="_blank" >http://dx.doi.org/10.1007/s00018-013-1450-x</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1007/s00018-013-1450-x" target="_blank" >10.1007/s00018-013-1450-x</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    CAS directly interacts with vinculin to control mechanosensing and focal adhesion dynamics

  • Original language description

    Focal adhesions are cellular structures through which both mechanical forces and regulatory signals are transmitted. Two focal adhesion-associated proteins, Crk-associated substrate (CAS) and vinculin, were both independently shown to be crucial for theability of cells to transmit mechanical forces and to regulate cytoskeletal tension. Here, we identify a novel, direct binding interaction between CAS and vinculin. This interaction is mediated by the CAS SRC homology 3 domain and a proline-rich sequencein the hinge region of vinculin. We show that CAS localization in focal adhesions is partially dependent on vinculin, and that CAS-vinculin coupling is required for stretch-induced activation of CAS at the Y410 phosphorylation site. Moreover, CAS-vinculin binding significantly affects the dynamics of CAS and vinculin within focal adhesions as well as the size of focal adhesions. Finally, disruption of CAS binding to vinculin reduces cell stiffness and traction force generation. Taken to

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    EB - Genetics and molecular biology

  • OECD FORD branch

Result continuities

  • Project

    <a href="/en/project/GC13-24851J" target="_blank" >GC13-24851J: Dissecting of BCAR1/CAS role in mechanosensing</a><br>

  • Continuities

    Z - Vyzkumny zamer (s odkazem do CEZ)<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2014

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Cellular and Molecular Life Sciences

  • ISSN

    1420-682X

  • e-ISSN

  • Volume of the periodical

    71

  • Issue of the periodical within the volume

    4

  • Country of publishing house

    CH - SWITZERLAND

  • Number of pages

    18

  • Pages from-to

    727-744

  • UT code for WoS article

    000330586500013

  • EID of the result in the Scopus database