Interaction of filamin A with the integrin β7 cytoplasmic domain: role of alternative splicing and phosphorylation
- 9 June 2004
- journal article
- Published by Wiley in FEBS Letters
- Vol. 569 (1-3) , 185-190
- https://doi.org/10.1016/j.febslet.2004.04.099
Abstract
Integrin-filamin binding plays an important role in adhesion-mediated control of the actin cytoskeleton. Here, using the interaction between recombinant fragments from the C-terminus of filamin A and the cytoplasmic tail of integrin beta 7 as a model, we report a negative regulatory role for filamin alternative splicing. Splice variant forms of filamin A lacking a 41-amino acid segment interacted more strongly than full-length fragments. In addition, we provide evidence that phosphorylation of the splice variant region is unlikely to represent the mechanism by which binding is reduced.Keywords
This publication has 25 references indexed in Scilit:
- NEW EMBO MEMBER'S REVIEW: The integrin-actin connection, an eternal love affairThe EMBO Journal, 2003
- An unraveling tale of how integrins are activated from withinTrends in Pharmacological Sciences, 2003
- IntegrinsCell, 2002
- Different splice variants of filamin-B affect myogenesis, subcellular distribution, and determine binding to integrin β subunitsThe Journal of cell biology, 2002
- Phosphorylation of the Integrin α4 Cytoplasmic Domain Regulates Paxillin BindingJournal of Biological Chemistry, 2001
- Calpain Cleavage Promotes Talin Binding to the β3Integrin Cytoplasmic DomainJournal of Biological Chemistry, 2001
- Sequence and structure-based prediction of eukaryotic protein phosphorylation sitesJournal of Molecular Biology, 1999
- Filamin Binds to the Cytoplasmic Domain of the β1-IntegrinJournal of Biological Chemistry, 1998
- Peptide ‘Velcro’: Design of a heterodimeric coiled coilCurrent Biology, 1993
- Human endothelial actin-binding protein (ABP-280, nonmuscle filamin): a molecular leaf spring.The Journal of cell biology, 1990