期刊
JOURNAL OF CELL SCIENCE
卷 119, 期 17, 页码 3561-3570出版社
COMPANY OF BIOLOGISTS LTD
DOI: 10.1242/jcs.03096
关键词
non-muscle myosin; myoblasts; fusion; antisense; muscle; electron microscopy
类别
资金
- Biotechnology and Biological Sciences Research Council [BB/D524875/1] Funding Source: researchfish
- BBSRC [BB/D524875/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/D524875/1] Funding Source: Medline
- Wellcome Trust Funding Source: Medline
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 nonmuscle 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. Nonmuscle 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 nonmuscle 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.
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