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MBC in Press, published online ahead of print February 6, 2003
Mol. Biol. Cell 10.1091/mbc.E03-01-0852

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Submitted on January 2, 2003
Accepted on January 30, 2003

Opposing roles of integrin {alpha}6A {beta}1 and dystroglycan in laminin-mediated ERK activation

Maria Ferletta1, Yamato Kikkawa1, Hao Yu2, Jan F. Talts2, Madeleine Durbeej3, Arnoud Sonnenberg4, Rupert Timpl5, Kevin P. Campbell3, Elke Genersch1, and Peter Ekblom1*

1 Departments of Cell and Molecular Biology, Uppsala and Lund University, Sweden
2 Department of Cell and Molecular Biology, Lund University, Sweden
3 Department of Physiology and Biophysics and Neurology, Howard Hughes Medical Institute, University of Iowa, Iowa City, Iowa, USA
4 The Netherlands Cancer Institute, Amsterdam, The Netherlands
5 Max-Planck-Institute for Biochemistry, Martinsried, Germany

* Corresponding author. E-mail address: Peter.Ekblom{at}medkem.lu.se.

Laminin-integrin interactions can in some settings activate the extracellular signal regulated kinases (ERKs) but the control mechanisms are poorly understood. Here, we studied ERK activation in response to two laminins isoforms (-1 and -10/11) in two epithelial cell lines. Both cell lines expressed {beta}1 containing integrins and dystroglycan but lacked integrin {alpha}6{beta}4. Antibody perturbation assays showed that both cell lines bound to laminin-10/11 via the {alpha}3{beta}1and {alpha}6{beta}1 integrins. Although laminin-10/11 was a stronger adhesion complex than laminin-1 for both cell lines, both laminins activated ERK in only one of the two cell lines. The ERK activation was mediated by integrin {alpha}6b1 and not by {alpha}3{beta}1 or dystroglycan. Instead, we found that dystroglycan-binding domains of both laminin-1 and -10/11 suppressed integrin {alpha}6{beta}1-mediated ERK activation. Moreover, the responding cell line expressed the two integrin {alpha}6 splice variants, {alpha}6A and {alpha}6B, whereas the non-responding cell line expressed only {alpha}6B. Furthermore, ERK activation was seen in cells transfected with the integrin {alpha}6A subunit, but not in {alpha}6B transfected cells. We conclude that laminin-1 and -10/11 share the ability to induce ERK activation, that this is regulated by integrin {alpha}6A{beta}1, and suggest a novel role for dystroglycan binding laminin domains as suppressors of this activation.




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