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First published online May 28, 2005
doi: 10.1242/10.1242/jcs.02397

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Close encounters: regulation of vertebrate skeletal myogenesis by cell-cell contact

Brookdale Department of Molecular, Cell and Developmental Biology, Mount Sinai School of Medicine, New York, NY 10029, USA

View larger version (33K): [in a new window]   Fig. 1. Model for a promyogenic cell-surface complex. A complex of CDO, BOC, neogenin and its ligand netrin-3, and N- and M-cadherins and the cadherin-associated proteins ß-catenin and -catenin is found at sites of myoblast cell-cell contact. A CDO/BOC ligand, whose uncertain existence is indicated by stripes, is also shown. Multiple signaling pathways emanate from this complex, resulting in activation of transcription factors that drive muscle-specific gene expression, including: heterodimers of myogenic bHLH factors (M) and E proteins (E), SRF and NFATc3; regulation of the actin cytoskeleton; and ultimately differentiation into multinucleated myofibers with functional sarcomeres. Note that the figure as drawn is not meant to imply any particular stoichiometry or complex formation between CDO, BOC and neogenin, or between these proteins and cadherins. Note also that, although CDO, BOC and neogenin are shown on one cell and their ligands on the other, all these proteins are produced by myoblasts, and the signals shown here may occur in a bidirectional fashion. Finally, signals generated by these adhesion molecules and receptors are expected to cooperate with signals derived from soluble factors and the extracellular matrix during myogenesis. See text for further information.