Abstract
![Graphic][1] Mutation of a neuronal transcription factor that activates neurons causes protein misfolding and aggregation (green) in worm muscle cells. MORIMOTO/CSHL An overactive neuron can cause protein aggregation in its target cell, according to new work by Susana Garcia,
Highlights
What happens within the muscle fiber? According to the prevailing model, all the myosin motors remain attached to actin filaments, and the elasticity of individual myosins accounts for this force reduction—like a rubber band, they pull less as they contract further
New work by Malcolm Irving (King’s College, London, UK), Vincenzo Lombardi (University of Florence, Italy), and colleagues shows that, on the contrary, myosins maintain a constant force during shortening
Those myosins remaining attached to actin continued to exert a steady force even as they changed shape. This previously described shape change is an active process that continuously maintains the motor force. These results are counter to a model proposed 50 years ago by Andrew Huxley, who suggested that the force reduction of a contracting muscle fiber was due to reduced force from individual myosins
Summary
New work by Malcolm Irving (King’s College, London, UK), Vincenzo Lombardi (University of Florence, Italy), and colleagues shows that, on the contrary, myosins maintain a constant force during shortening. According to the prevailing model, all the myosin motors remain attached to actin filaments, and the elasticity of individual myosins accounts for this force reduction—like a rubber band, they pull less as they contract further. Not weaker, myosins reduce the overall muscle force during shortening. The authors combined precise mechanical measurements of individual muscle fibers with real-time x-ray diffraction, allowing them to measure myosin’s force and
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