Interaction of filamin A with the integrin β7 cytoplasmic domain:: role of alternative splicing and phosphorylation

Integrin-filamin binding plays an important role in adhesion-mediated control of the actin cytoskeleton. Here, using the interaction between recombinant fragments from the G 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. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.