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

Mark A. Travis; Arjan Van Der Flier; Richard A. Kammerer; A. Paul Mould; Arnoud Sonnenberg; Martin J. Humphries

doi:10.1016/j.febslet.2004.04.099

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

Mark A. Travis, Arjan Van Der Flier, Richard A. Kammerer, A. Paul Mould, Arnoud Sonnenberg, Martin J. Humphries

Research output: Contribution to journal › Article › peer-review

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 β7 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. © 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Original language	English
Pages (from-to)	185-190
Number of pages	5
Journal	FEBS Letters
Volume	569
Issue number	1-3
DOIs	https://doi.org/10.1016/j.febslet.2004.04.099
Publication status	Published - 2 Jul 2004

Keywords

Cell migration
Cytoskeleton
Filamin
Integrin
Splice variant

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10.1016/j.febslet.2004.04.099

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title = "Interaction of filamin A with the integrin β7 cytoplasmic domain: Role of alternative splicing and phosphorylation",

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 β7 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. {\textcopyright} 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.",

keywords = "Cell migration, Cytoskeleton, Filamin, Integrin, Splice variant",

author = "Travis, {Mark A.} and {Van Der Flier}, Arjan and Kammerer, {Richard A.} and Mould, {A. Paul} and Arnoud Sonnenberg and Humphries, {Martin J.}",

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doi = "10.1016/j.febslet.2004.04.099",

language = "English",

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T1 - Interaction of filamin A with the integrin β7 cytoplasmic domain: Role of alternative splicing and phosphorylation

AU - Travis, Mark A.

AU - Van Der Flier, Arjan

AU - Kammerer, Richard A.

AU - Mould, A. Paul

AU - Sonnenberg, Arnoud

AU - Humphries, Martin J.

PY - 2004/7/2

Y1 - 2004/7/2

N2 - 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 β7 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. © 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

AB - 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 β7 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. © 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

KW - Cell migration

KW - Cytoskeleton

KW - Filamin

KW - Integrin

KW - Splice variant

U2 - 10.1016/j.febslet.2004.04.099

DO - 10.1016/j.febslet.2004.04.099

M3 - Article

C2 - 15225631

VL - 569

SP - 185

EP - 190

JO - FEBS Letters

JF - FEBS Letters

IS - 1-3

ER -

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

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Keywords

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