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PMID: 15225631 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

FEBS letters ·Vol. 569 ·No. 1-3 ·2004-07-02 ·Pages 185-90

Travis MA, van der Flier A, Kammerer RA, Mould AP, Sonnenberg A, Humphries MJ

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.

MeSH Terms
Alternative Splicing/genetics Amino Acid Sequence Amino Acid Substitution Animals Binding Sites COS Cells Chlorocebus aethiops Contractile Proteins/chemistry,genetics,metabolism DNA, Complementary Filamins Integrin beta Chains/chemistry,genetics,metabolism Microfilament Proteins/chemistry,genetics,metabolism Molecular Sequence Data Mutagenesis, Site-Directed Peptide Fragments Phosphorylation Polymerase Chain Reaction/methods Recombinant Proteins/chemistry,metabolism Restriction Mapping Sequence Deletion Transfection
Chemicals
Contractile Proteins DNA, Complementary Filamins Integrin beta Chains Microfilament Proteins Peptide Fragments Recombinant Proteins integrin beta7
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Travis Mark A
School of Biological Sciences, 2.205 Stopford Building, Wellcome Trust Centre for Cell-Matrix Research, University of Manchester, The Michael Smith Building, Oxford Road, Manchester M13 9PT, UK.
van der Flier Arjan
Kammerer Richard A
Mould A Paul
Sonnenberg Arnoud
Humphries Martin J
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
2004-07-02
Pages
185-90
Language
English
Region
England
NLM ID
0155157
Subset
IM
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