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  Opposing roles of integrin alpha 6A beta 1 and dystroglycan in laminin-mediated extracellular signal-regulated kinase activation

Ferletta, M., Kikkawa, Y., Yu, H., Talts, J. F., Durbeej, M., Sonnenberg, A., et al. (2003). Opposing roles of integrin alpha 6A beta 1 and dystroglycan in laminin-mediated extracellular signal-regulated kinase activation. Molecular Biology of the Cell, 14(5), 2088-2103.

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Genre: Journal Article
Alternative Title : Mol. Biol. Cell

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 Creators:
Ferletta, M., Author
Kikkawa, Y., Author
Yu, H., Author
Talts, J. F., Author
Durbeej, M., Author
Sonnenberg, A., Author
Timpl, R.1, Author           
Campbell, K. P., Author
Ekblom, P., Author
Genersch, E., Author
Affiliations:
1Former Research Groups, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565145              

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 Abstract: Laminin-integrin interactions can in some settings activate the extracellular signal-regulated kinases (ERKs) but the control mechanisms are poorly understood. Herein, we studied ERK activation in response to two laminins isoforms (-1 and -10/11) in two epithelial cell lines. Both cell lines expressed beta1- containing integrins and dystroglycan but lacked integrin alpha6beta4. Antibody perturbation assays showed that both cell lines bound to laminin-10/11 via the alpha3beta1and alpha6beta1 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 alpha6beta1 and not by 001 or dystroglycan. Instead, we found that dystroglycan-binding domains of both laminin-1 and -10/11 suppressed integrin a6pl- mediated ERK activation. Moreover, the responding cell line expressed the two integrin alpha6 splice variants, alpha6A and alpha6B, whereas the nonresponding cell line expressed only a6B. Furthermore, ERK activation was seen in cells transfected with the integrin alpha6A subunit, but not in alpha6B- transfected cells. We conclude that laminin-1 and -10/11 share the ability to induce ERK activation, that this is regulated by integrin alpha6Abeta1, and suggest a novel role for dystroglycan-binding laminin domains as suppressors of this activation.

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Language(s): eng - English
 Dates: 2003-05
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 41361
ISI: 000182907100029
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Title: Molecular Biology of the Cell
  Alternative Title : Mol. Biol. Cell
Source Genre: Journal
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Pages: - Volume / Issue: 14 (5) Sequence Number: - Start / End Page: 2088 - 2103 Identifier: ISSN: 1059-1524