Article (Scientific journals)
Distinct involvement of beta3 integrin cytoplasmic domain tyrosine residues 747 and 759 in integrin-mediated cytoskeletal assembly and phosphotyrosine signaling.
SCHAFFNER-RECKINGER, Elisabeth; Gouon, V.; MELCHIOR, Chantal et al.
1998In The Journal of biological chemistry, 273 (20), p. 12623-32
Peer reviewed
 

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Keywords :
Amino Acid Sequence; Animals; Antigens, CD/chemistry/metabolism; CHO Cells; Cell Adhesion Molecules/metabolism; Cell Movement; Cricetinae; Cytoplasm/metabolism; Cytoskeleton/metabolism; Fibrinogen/metabolism; Focal Adhesion Protein-Tyrosine Kinases; Integrin beta3; Molecular Sequence Data; Phosphorylation; Phosphotyrosine/metabolism; Platelet Membrane Glycoproteins/chemistry/metabolism; Protein-Tyrosine Kinases/metabolism; Sequence Homology, Amino Acid; Signal Transduction
Abstract :
[en] We have investigated the structural requirements of the beta3 integrin subunit cytoplasmic domain necessary for tyrosine phosphorylation of focal adhesion kinase (FAK) and paxillin during alphav beta3-mediated cell spreading. Using CHO cells transfected with various beta3 mutants, we demonstrate a close correlation between alphav beta3-mediated cell spreading and tyrosine phosphorylation of FAK and paxillin, and highlight a distinct involvement of the NPLY747 and NITY759 motifs in these signaling processes. Deletion of the NITY759 motif alone was sufficient to completely prevent alphav beta3-dependent focal contact formation, cell spreading, and FAK/paxillin phosphorylation. The single Y759A substitution induced a strong inhibitory phenotype, while the more conservative, but still phosphorylation-defective, Y759F mutation restored wild type receptor function. Alanine substitution of the highly conserved Tyr747 completely abolished alphav beta3-dependent formation of focal adhesion plaques, cell spreading, and FAK/paxillin phosphorylation, whereas a Y747F substitution only partially restored these events. As none of these mutations affected receptor-ligand interaction, our results suggest that the structural integrity of the NITY759 motif, rather than the phosphorylation status of Tyr759 is important for beta3-mediated cytoskeleton reorganization and tyrosine phosphorylation of FAK and paxillin, while the presence of Tyr at residue 747 within the NPLY747 motif is required for optimal beta3 post-ligand binding events.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
SCHAFFNER-RECKINGER, Elisabeth ;  University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > Life Science Research Unit
Gouon, V.
MELCHIOR, Chantal 
PLANÇON, Sébastien ;  University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > Life Science Research Unit
Kieffer, N.
Language :
English
Title :
Distinct involvement of beta3 integrin cytoplasmic domain tyrosine residues 747 and 759 in integrin-mediated cytoskeletal assembly and phosphotyrosine signaling.
Publication date :
1998
Journal title :
The Journal of biological chemistry
ISSN :
0021-9258
Volume :
273
Issue :
20
Pages :
12623-32
Peer reviewed :
Peer reviewed
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since 14 October 2013

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