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          Institute: MPI für Biochemie     Collection: Emeriti Groups     Display Documents



ID: 41361.0, MPI für Biochemie / Emeriti Groups
Opposing roles of integrin alpha 6A beta 1 and dystroglycan in laminin-mediated extracellular signal-regulated kinase activation
Authors:Ferletta, M.; Kikkawa, Y.; Yu, H.; Talts, J. F.; Durbeej, M.; Sonnenberg, A.; Timpl, R.; Campbell, K. P.; Ekblom, P.; Genersch, E.
Language:English
Date of Publication (YYYY-MM-DD):2003-05
Title of Journal:Molecular Biology of the Cell
Journal Abbrev.:Mol. Biol. Cell
Volume:14
Issue / Number:5
Start Page:2088
End Page:2103
Review Status:Peer-review
Audience:Not Specified
Abstract / Description: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.
Comment of the Author/Creator:Date: 2003, MAY
External Publication Status:published
Document Type:Article
Communicated by:N.N.
Affiliations:MPI für Biochemie/Emeriti Groups/Protein Chemistry (R. Timpl)
External Affiliations:Univ Uppsala, Dept Cell & Mol Biol, SE-75123 Uppsala, Sweden; Univ Uppsala, Dept Cell & Mol Biol, SE-75123 Uppsala, Sweden; Lund Univ, Dept Cell & Mol Biol, SE-22184 Lund, Sweden; Univ Iowa, Howard Hughes Med Inst, Dept Physiol Biophys & Neurol, Iowa City, IA 52242 USA; Netherlands Canc Inst, Amsterdam, Netherlands
Identifiers:ISI:000182907100029 [ID No:1]
ISSN:1059-1524 [ID No:2]
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