期刊
NANO LETTERS
卷 15, 期 4, 页码 2220-2228出版社
AMER CHEMICAL SOC
DOI: 10.1021/nl5047335
关键词
Mechanobiology; integrin; focal adhesion; molecular tension sensor; super-resolution; traction force microscopy
类别
资金
- Stanford Bio-X TIP award
- National Science Foundation (NSF) under Emerging Frontiers in Research and Innovation (EFRI) [1136790]
- National Institute of Health (NTH) New Innovator Award [1DP20D007078]
- Stanford Cardiovascular Institute Seed Grant
- Burroughs-Wellcome Career Award at the Scientific Interface
- NSF Graduate Research Fellowships [1000121811, 1000125096]
- Stanford Graduate Fellowship
- National Center for Research Resources (NCRR) [1S100D01277601]
Focal adhesions (FAs) are micron-sized protein assemblies that coordinate cell adhesion, migration, and mechanotransduction. How the many proteins within FAs are organized into force sensing and transmitting structures is poorly understood. We combined fluorescent molecular tension sensors with super-resolution light microscopy to visualize traction forces within FAs with <100 nm spatial resolution. We find that alpha(v)beta(3) integrin selectively localizes to high force regions. Paxillin, which is not generally considered to play a direct role in force transmission, shows a higher degree of spatial correlation with force than vinculin, talin, or alpha-actinin, proteins with hypothesized roles as force transducers. These observations suggest that alpha(v)beta(3) integrin and paxillin may play important roles in mechanotransduction.
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