Interaction of filamin A with the integrin beta 7 cytoplasmic domain: role of alternative splicing and phosphorylation.

  • Travis M
  • van der Flier A
  • Kammerer R
 et al. 
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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.

Author-supplied keywords

  • Alternative Splicing
  • Alternative Splicing: genetics
  • Amino Acid Sequence
  • Amino Acid Substitution
  • Animals
  • Binding Sites
  • COS Cells
  • Cercopithecus aethiops
  • Contractile Proteins
  • Contractile Proteins: chemistry
  • Contractile Proteins: genetics
  • Contractile Proteins: metabolism
  • DNA, Complementary
  • Integrin beta Chains
  • Integrin beta Chains: chemistry
  • Integrin beta Chains: genetics
  • Integrin beta Chains: metabolism
  • Microfilament Proteins
  • Microfilament Proteins: chemistry
  • Microfilament Proteins: genetics
  • Microfilament Proteins: metabolism
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Peptide Fragments
  • Phosphorylation
  • Polymerase Chain Reaction
  • Polymerase Chain Reaction: methods
  • Recombinant Proteins
  • Recombinant Proteins: chemistry
  • Recombinant Proteins: metabolism
  • Restriction Mapping
  • Sequence Deletion
  • Transfection

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  • Mark a Travis

  • Arjan van der Flier

  • Richard a Kammerer

  • a Paul Mould

  • Arnoud Sonnenberg

  • Martin J Humphries

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