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@ARTICLE{Smith:400,
author = {Smith, A. and Sengupta, K. and Goennewein, S. and Seifert,
U. and Sackmann, E.},
title = {{F}orce-induced growth of adhesion domains is controlled by
receptor mobility},
journal = {Proceedings of the National Academy of Sciences of the
United States of America},
volume = {105},
issn = {0027-8424},
address = {Washington, DC},
publisher = {Academy},
reportid = {PreJuSER-400},
pages = {6906 - 6911},
year = {2008},
note = {Record converted from VDB: 12.11.2012},
abstract = {In living cells, adhesion structures have the astonishing
ability to grow and strengthen under force. Despite the
rising evidence of the importance of this phenomenon, little
is known about the underlying mechanism. Here, we show that
force-induced adhesion-strengthening can occur purely
because of the thermodynamic response to the elastic
deformation of the membrane, even in the absence of the
actively regulated cytoskeleton of the cell, which was
hitherto deemed necessary. We impose pN-forces on two fluid
membranes, locally pre-adhered by RGD-integrin binding. One
of the binding partners is always mobile whereas the
mobility of the other can be switched on or off. Immediate
passive strengthening of adhesion structures occurs in both
cases. When both binding partners are mobile, strengthening
is aided by lateral movement of intact bonds as a transient
response to force-induced membrane-deformation. By extending
our microinterferometric technique to the suboptical regime,
we show that the adhesion, as well as the resistance to
force-induced de-adhesion, is greatly enhanced when both,
rather than only one, of the binding partners are mobile. We
formulate a theory that explains our observations by linking
the macroscopic shape deformation with the microscopic
formation of bonds, which further elucidates the importance
of receptor mobility. We propose this fast passive response
to be the first-recognition that triggers signaling events
leading to mechanosensing in living cells.},
keywords = {Biomechanics / Cell Adhesion / Elasticity / Integrins:
metabolism / Models, Biological / Oligopeptides: metabolism
/ Protein Transport / Unilamellar Liposomes: metabolism /
Integrins (NLM Chemicals) / Oligopeptides (NLM Chemicals) /
Unilamellar Liposomes (NLM Chemicals) /
arginyl-glycyl-aspartic acid (NLM Chemicals) / J (WoSType)},
cin = {IBN-4},
ddc = {000},
cid = {I:(DE-Juel1)VDB802},
pnm = {Kondensierte Materie},
pid = {G:(DE-Juel1)FUEK414},
shelfmark = {Multidisciplinary Sciences},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:18463289},
pmc = {pmc:PMC2383988},
UT = {WOS:000255921200023},
doi = {10.1073/pnas.0801706105},
url = {https://juser.fz-juelich.de/record/400},
}