Article (Scientific journals)
The talin rod IBS2 alpha-helix interacts with the beta3 integrin cytoplasmic tail membrane-proximal helix by establishing charge complementary salt bridges.
Rodius, Sophie; Chaloin, Olivier; MOES, Michèle et al.
2008In The Journal of biological chemistry, 283 (35), p. 24212-23
Peer reviewed
 

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Keywords :
Actin Cytoskeleton/chemistry/genetics/metabolism; Animals; CHO Cells; Cricetinae; Cricetulus; Humans; Integrin beta3/chemistry/genetics/metabolism; Models, Molecular; Peptide Mapping/methods; Platelet Membrane Glycoprotein IIb/chemistry/genetics/metabolism; Protein Binding/physiology; Protein Structure, Secondary/physiology; Protein Structure, Tertiary/physiology; Talin/chemistry/genetics/metabolism
Abstract :
[en] Talin establishes a major link between integrins and actin filaments and contains two distinct integrin binding sites: one, IBS1, located in the talin head domain and involved in integrin activation and a second, IBS2, that maps to helix 50 of the talin rod domain and is essential for linking integrin beta subunits to the cytoskeleton ( Moes, M., Rodius, S., Coleman, S. J., Monkley, S. J., Goormaghtigh, E., Tremuth, L., Kox, C., van der Holst, P. P., Critchley, D. R., and Kieffer, N. (2007) J. Biol. Chem. 282, 17280-17288 ). Through the combined approach of mutational analysis of the beta3 integrin cytoplasmic tail and the talin rod IBS2 site, SPR binding studies, as well as site-specific antibody inhibition experiments, we provide evidence that the integrin beta3-talin rod interaction relies on a helix-helix association between alpha-helix 50 of the talin rod domain and the membrane-proximal alpha-helix of the beta3 integrin cytoplasmic tail. Moreover, charge complementarity between the highly conserved talin rod IBS2 lysine residues and integrin beta3 glutamic acid residues is necessary for this interaction. Our results support a model in which talin IBS2 binds to the same face of the beta3 subunit cytoplasmic helix as the integrin alphaIIb cytoplasmic tail helix, suggesting that IBS2 can only interact with the beta3 subunit following integrin activation.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Rodius, Sophie
Chaloin, Olivier
MOES, Michèle ;  University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > Life Science Research Unit
SCHAFFNER-RECKINGER, Elisabeth ;  University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > Life Science Research Unit
Landrieu, Isabelle
Lippens, Guy
Lin, Minghui
ZHANG, Jie ;  University of Luxembourg > Luxembourg Centre for Systems Biomedicine (LCSB)
KIEFFER, Nelly 
Language :
English
Title :
The talin rod IBS2 alpha-helix interacts with the beta3 integrin cytoplasmic tail membrane-proximal helix by establishing charge complementary salt bridges.
Publication date :
2008
Journal title :
The Journal of biological chemistry
ISSN :
0021-9258
Volume :
283
Issue :
35
Pages :
24212-23
Peer reviewed :
Peer reviewed
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