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First published online 8 August 2006
doi: 10.1242/jcs.03096

Journal of Cell Science 119, 3561-3570 (2006)
Published by The Company of Biologists 2006
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Research Article

Non-muscle myosins 2A and 2B drive changes in cell morphology that occur as myoblasts align and fuse

Nathan T. Swailes*, Melanie Colegrave, Peter J. Knight and Michelle Peckham{ddagger}

Institute of Molecular and Cellular Biology, University of Leeds, Leeds, LS2 9JT, UK

{ddagger} Author for correspondence (e-mail: m.peckham{at}leeds.ac.uk)

Accepted 12 June 2006

The interaction of non-muscle myosins 2A and 2B with actin may drive changes in cell movement, shape and adhesion. To investigate this, we used cultured myoblasts as a model system. These cells characteristically change shape from triangular to bipolar when they form groups of aligned cells. Antisense oligonucleotide knockdown of non-muscle myosin 2A, but not non-muscle myosin 2B, inhibited this shape change, interfered with cell-cell adhesion, had a minor effect on tail retraction and prevented myoblast fusion. By contrast, non-muscle myosin 2B knockdown markedly inhibited tail retraction, increasing cell length by over 200% by 72 hours compared with controls. In addition it interfered with nuclei redistribution in myotubes. Non-muscle myosin 2C is not involved as western analysis showed that it is not expressed in myoblasts, but only in myotubes. To understand why non-muscle myosins 2A and 2B have such different roles, we analysed their distributions by immuno-electron microscopy, and found that non-muscle myosin 2A was more tightly associated with the plasma membrane than non-muscle myosin 2B. This suggests that non-muscle myosin 2A is more important for bipolar shape formation and adhesion owing to its preferential interaction with membrane-associated actin, whereas the role of non-muscle myosin 2B in retraction prevents over-elongation of myoblasts.

Key words: Non-muscle myosin, Myoblasts, Fusion, Antisense, Muscle, Electron microscopy




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