Journal
ACS NANO
Volume 10, Issue 12, Pages 10745-10752Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acsnano.6b03314
Keywords
integrin; cell adhesion; mechanobiology; single molecule; tension sensor
Categories
Funding
- National Institute of Health (NIH) [1R01GM11299801]
- Stanford Bio-X IIP award
- National Science Foundation (NSF) under Emerging Frontiers in Research and Innovation (EFRI) [1136790]
- NIH New Innovator Award [1DP2OD007078]
- NIH [R21HL13099301]
- NSF Graduate Research Fellowships
- Grants-in-Aid for Scientific Research [16K16387] Funding Source: KAKEN
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Integrins mediate cell adhesion to the extracellular matrix and enable the construction of complex, multicellular organisms, yet fundamental aspects of integrin-based adhesion remain poorly understood. Notably, the magnitude of the mechanical load experienced by individual integrins within living cells is unclear, due principally to limitations inherent to existing techniques. Here we use Forster resonance energy transfer-based molecular tension sensors to directly measure the distribution of loads experienced by individual integrins in living cells. We find that a large fraction of integrins bear modest loads of 1-3 pN, while subpopulations bearing higher loads are enriched within adhesions. Further, our data indicate that integrin engagement with the fibronectin synergy site, a secondary binding site specifically for alpha(5)beta(1) integrin, leads to increased levels of alpha(5)beta(1) integrin recruitment to adhesions but not to an increase in overall cellular traction generation. The presence of the synergy site does, however, increase cells' resistance to detachment by externally applied loads. We suggest that a substantial population of integrins experiencing loads well below their peak capacities can provide cells and tissues with mechanical integrity in the presence of widely varying mechanical loads.
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