JBC 2010 – Myosin Motors Drive Long Range Alignment of Actin Filaments

| February 12, 2010

Tariq Butt, Tabish Mufti, Ahmad Humayun, Peter B. Rosenthal, Sohaib Khan, Shahid Khan, Justin E. Molloy
Journal of Biological Chemistry, Vol 285, No 7, Feb 12, 2010 


The bulk alignment of actin filament sliding movement, powered by randomly oriented myosin molecules, has been observed and studied using an in vitro motility assay. The well established, actin filament gliding assay is a minimal experimental system for studying actomyosin motility. Here, we show that when the assay is performed at densities of actin filaments approaching those found in living cells, filament gliding takes up a preferred orientation. The oriented patterns of movement that we have observed extend over a length scale of 10 –100 μm, similar to the size of a mammalian cell. We studied the process of filament alignment and found that it depends critically upon filament length and density. We developed a simple quantitative measure of filament sliding orientation and this enabled us to follow the time course of alignment and the formation and disappearance of oriented domains. Domains of oriented filaments formed spontaneously and were separated by distinct boundaries. The pattern of the domain structures changed on the time scale of several seconds and the collision of neighboring domains led to emergence of new patterns. Our results indicate that actin filament crowding may play an important role in structuring the leading edge of migrating cells. Filament alignment due to near-neighbor mechanical interactions can propagate over a length scale of several microns; much greater than the size of individual filaments and analogous to a log drive. Self-alignment of actin filaments may make an important contribution to cell polarity and provide a mechanism by which cell migration direction responds to chemical cues.


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Text Reference:

Tariq Butt, Tabish Mufti, Ahmad Humayun, Peter B. Rosenthal, Sohaib Khan,
Shahid Khan, Justin E. Molloy
"Myosin Motors Drive Long Range Alignment of Actin Filaments"
Journal of Biological Chemistry, Vol. 285, No. 7, pp. 4964-4974, Feb 12, 2010

Bibtex Reference:

  title={Myosin motors drive long range alignment of actin filaments},
  author={Butt, T. and Mufti, T. and Humayun, A. and Rosenthal, P.B. and Khan, S.
and Khan, S. and Molloy, J.E.},
  journal={Journal of Biological Chemistry},


these are looser and not so short
ddtankMaggie Lane WOMEN’S MILITARY HAT

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Category: Journal Papers, Publications

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