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Kinetic regulation of beta 3 integrin tyrosine phosphorylation
- Source :
- The Journal of biological chemistry. 277(49)
- Publication Year :
- 2002
-
Abstract
- Tyrosine phosphorylation of beta(3) integrins is a permissive stage in the activation of alpha(IIb)beta(3) and alpha(v)beta(3) in platelets and leukocytes, respectively. In this study we demonstrated direct phosphorylation of beta(3) integrins as a result of interaction with soluble monomeric ligand, and we characterized the differential kinetics of beta(3) phosphorylation as a consequence of alpha subunit pairing. We found that beta(3) phosphorylation is initiated by RGD peptide binding in a dose-dependent and saturable fashion with alpha(IIb)beta(3) becoming phosphorylated and dephosphorylated more rapidly than alpha(v)beta(3). Site mapping of phosphate incorporation reveals significant phosphorylation at Tyr-747 in both beta(3) integrin species with incorporation at Tyr-759 found at significant levels only in alpha(IIb)beta(3). Mutation of cytoplasmic beta(3) tyrosine residues in a transfection model prevents cell adhesion via these integrins. These data demonstrate that recognition of ligand is sufficient to induce beta(3) tyrosine phosphorylation and suggests that this event is regulated by the alpha subunit pairing of beta(3).
- Subjects :
- inorganic chemicals
Cytoplasm
Time Factors
Integrin
macromolecular substances
Protein tyrosine phosphatase
Ligands
Transfection
Biochemistry
Phosphorylation cascade
chemistry.chemical_compound
Mice
Cell Adhesion
Animals
Humans
Protein phosphorylation
Tyrosine
Phosphorylation
Cell adhesion
Molecular Biology
Binding Sites
biology
Dose-Response Relationship, Drug
Integrin beta3
Tyrosine phosphorylation
Cell Biology
Flow Cytometry
Integrin alphaVbeta3
Cell biology
enzymes and coenzymes (carbohydrates)
Kinetics
chemistry
Gene Expression Regulation
Mutation
biology.protein
K562 Cells
Peptides
Oligopeptides
Protein Binding
Subjects
Details
- ISSN :
- 00219258
- Volume :
- 277
- Issue :
- 49
- Database :
- OpenAIRE
- Journal :
- The Journal of biological chemistry
- Accession number :
- edsair.doi.dedup.....2c4616739e4a55158d57b3371658c0ed