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First published online 28 April 2009
doi: 10.1242/jcs.046219

Journal of Cell Science 122, 1637-1646 (2009)
Published by The Company of Biologists 2009
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Research Article

The collagen receptor DDR1 regulates cell spreading and motility by associating with myosin IIA

Yun Huang1, Pamela Arora2, Christopher A. McCulloch2,* and Wolfgang F. Vogel1,{ddagger}

1 Department of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, Ontario M5S 1A8, Canada
2 Canadian Institutes of Health Research Group in Matrix Dynamics, University of Toronto, Toronto, Ontario M5S 3E2, Canada

* Author for correspondence (e-mail: christopher.mcculloch{at}utoronto.ca)

Accepted 9 February 2009

The spreading and migration of cells on adhesive substrates is regulated by the counterbalance of contractile and protrusive forces. Non-muscle myosin IIA, an ubiquitously expressed contractile protein and enzyme, is implicated in the regulation of cell spreading and directional migration in response to various stimuli. Here we show that discoidin domain receptor 1 (DDR1), a tyrosine kinase receptor activated by type I collagen, associates with the non-muscle myosin IIA heavy chain (NMHC-IIA) upon ligand stimulation. An association was also indicated by coimmunoprecipitation of NMHC-IIA with full-length DDR1, but not with the truncated DDR1d-isoform lacking the kinase domain. DDR1 was important for assembly of NMHC-IIA into filaments on cells plated on collagen. DDR1 expression inhibited cell spreading over collagen but promoted cell migration. By contrast, blockade of non-muscle myosin II activity by blebbistatin enhanced cell spreading but inhibited migration over collagen. We propose that myosin and DDR1 impact cell spreading and migration by regulating adhesive contacts with collagen.

Key words: Actin, Discoidin domain receptor, Integrin, Migration, Non-muscle myosin IIA, Cell spreading


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