Differential association of cytoplasmic signalling molecules SHP-1, SHP-2, SHIP and phospholipase C-gamma1 with PECAM-1/CD31.
Recent studies have shown that, in addition to its role as an adhesion receptor, platelet endothelial cell adhesion molecule 1/CD31 becomes phosphorylated on tyrosine residues Y663 and Y686 and associates with protein tyrosine phosphatases SHP-1 and SHP-2. In this study, we screened for additional proteins which associate with phosphorylated platelet ... endothelial cell adhesion molecule 1, using surface plasmon resonance. We found that, besides SHP-1 and SHP-2, platelet endothelial cell adhesion molecule 1 binds the cytoplasmic signalling proteins SHIP and PLC-gamma1 via their Src homology 2 domains. Using two phosphopeptides, NSDVQpY663TEVQV and DTETVpY686SEVRK, we demonstrate differential binding of SHP-1, SHP-2, SHIP and PLC-gamma1. All four cytoplasmic signalling proteins directly associate with cellular platelet endothelial cell adhesion molecule 1, immunoprecipitated from pervanadate-stimulated THP-1 cells. These results suggest that overlapping immunoreceptor tyrosine-based inhibition motif/immunoreceptor tyrosine-based activation motif-like motifs within platelet endothelial cell adhesion molecule 1 mediate differential interactions between the Src homology 2 containing signalling proteins SHP-1, SHP-2, SHIP and PLC-gamma1.
Mesh Terms:
Amino Acid Sequence, Antigens, CD31, Binding Sites, Humans, Intracellular Signaling Peptides and Proteins, Isoenzymes, Molecular Sequence Data, Monocytes, Phospholipase C gamma, Phosphopeptides, Phosphoric Monoester Hydrolases, Phosphorylation, Phosphotyrosine, Protein Binding, Protein Tyrosine Phosphatase, Non-Receptor Type 11, Protein Tyrosine Phosphatase, Non-Receptor Type 6, Protein Tyrosine Phosphatases, SH2 Domain-Containing Protein Tyrosine Phosphatases, Sequence Homology, Amino Acid, Signal Transduction, Surface Plasmon Resonance, Type C Phospholipases, Vanadates, src Homology Domains
Amino Acid Sequence, Antigens, CD31, Binding Sites, Humans, Intracellular Signaling Peptides and Proteins, Isoenzymes, Molecular Sequence Data, Monocytes, Phospholipase C gamma, Phosphopeptides, Phosphoric Monoester Hydrolases, Phosphorylation, Phosphotyrosine, Protein Binding, Protein Tyrosine Phosphatase, Non-Receptor Type 11, Protein Tyrosine Phosphatase, Non-Receptor Type 6, Protein Tyrosine Phosphatases, SH2 Domain-Containing Protein Tyrosine Phosphatases, Sequence Homology, Amino Acid, Signal Transduction, Surface Plasmon Resonance, Type C Phospholipases, Vanadates, src Homology Domains
FEBS Lett.
Date: Apr. 30, 1999
PubMed ID: 10350061
View in: Pubmed Google Scholar
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