Myosin IC generates power over a range of loads via a new tension-sensing mechanism

@article{Greenberg2012MyosinIG,
  title={Myosin IC generates power over a range of loads via a new tension-sensing mechanism},
  author={M. Greenberg and Tianming Lin and Y. Goldman and H. Shuman and E. Ostap},
  journal={Proceedings of the National Academy of Sciences},
  year={2012},
  volume={109},
  pages={E2433 - E2440}
}
Myosin IC (myo1c), a widely expressed motor protein that links the actin cytoskeleton to cell membranes, has been associated with numerous cellular processes, including insulin-stimulated transport of GLUT4, mechanosensation in sensory hair cells, endocytosis, transcription of DNA in the nucleus, exocytosis, and membrane trafficking. The molecular role of myo1c in these processes has not been defined, so to better understand myo1c function, we utilized ensemble kinetic and single-molecule… Expand
Mechanochemical tuning of myosin-I by the N-terminal region
Myosin-10 produces its power-stroke in two phases and moves processively along a single actin filament under low load
A Perspective on the Role of Myosins as Mechanosensors.
Motor and tail homology 1 (Th1) domains antagonistically control myosin-1 dynamics.
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 59 REFERENCES
Control of myosin-I force sensing by alternative splicing
Calcium regulation of myosin-I tension sensing.
Myosin I Can Act As a Molecular Force Sensor
Load-dependent kinetics of myosin-V can explain its high processivity
The kinetic mechanism of myosin V.
Robust mechanosensing and tension generation by myosin VI.
The motor protein myosin-I produces its working stroke in two steps
Contribution of the myosin VI tail domain to processive stepping and intramolecular tension sensing
Single kinesin molecules studied with a molecular force clamp
Force generation in single conventional actomyosin complexes under high dynamic load.
...
1
2
3
4
5
...