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Myosin IIB assembly state determines its mechanosensitive dynamics.

Eric S Schiffhauer1, Yixin Ren1, Vicente A Iglesias2

  • 1Department of Cell Biology, School of Medicine, Johns Hopkins University, Baltimore, MD.

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|January 19, 2019
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Cellular myosin II (a motor protein) mechanoresponsiveness is biphasic, optimized by filament assembly. Its assembly state, influenced by phosphorylation and expression, governs cellular mechanical responses.

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Area of Science:

  • Cell Biology
  • Biophysics
  • Biochemistry

Background:

  • Cellular dynamics and shape changes rely on systems sensitive to chemical and mechanical cues.
  • Myosin II motors are crucial for cellular mechanical responses, notably accumulating under stress.

Purpose of the Study:

  • To investigate how myosin II filament assembly state affects its response to mechanical stress.
  • To model and predict the relationship between myosin II assembly and mechanoresponsiveness.

Main Methods:

  • Mathematical modeling of myosin II in *Dictyostelium*.
  • Experimental analysis in HeLa and NIH 3T3 cells.

Main Results:

  • Mathematical modeling predicted a biphasic myosin II mechanoresponsiveness, with an optimal response at a specific bipolar filament assembly percentage.
  • Phosphorylation of NMIIB by PKCζ and NMIIA expression were shown to modulate NMIIB's assembly state and mechanoresponse in mammalian cells.

Conclusions:

  • Myosin II mechanoresponsiveness is intrinsically linked to its filament assembly state.
  • Multiple cellular inputs converge on myosin II assembly, regulating the cell's response to mechanical stimuli.