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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Alternative Splicing / genetics*
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Amino Acid Sequence
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Amino Acid Substitution
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Animals
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Binding Sites
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COS Cells
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Chlorocebus aethiops
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Contractile Proteins / chemistry
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Contractile Proteins / genetics
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Contractile Proteins / metabolism*
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DNA, Complementary
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Filamins
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Integrin beta Chains / chemistry
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Integrin beta Chains / genetics
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Integrin beta Chains / metabolism*
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Microfilament Proteins / chemistry
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Microfilament Proteins / genetics
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Microfilament Proteins / metabolism*
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Molecular Sequence Data
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Mutagenesis, Site-Directed
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Peptide Fragments
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Phosphorylation
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Polymerase Chain Reaction / methods
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Restriction Mapping
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Sequence Deletion
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Transfection
Substances
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Contractile Proteins
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DNA, Complementary
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Filamins
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Integrin beta Chains
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Microfilament Proteins
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Peptide Fragments
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Recombinant Proteins
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integrin beta7