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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.

Original publication

DOI

10.1016/s0014-5793(99)00446-9

Type

Journal article

Journal

FEBS Lett

Publication Date

30/04/1999

Volume

450

Pages

77 - 83

Keywords

Amino Acid Sequence, Binding Sites, Humans, Intracellular Signaling Peptides and Proteins, Isoenzymes, Molecular Sequence Data, Monocytes, Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases, Phospholipase C gamma, Phosphopeptides, Phosphoric Monoester Hydrolases, Phosphorylation, Phosphotyrosine, Platelet Endothelial Cell Adhesion Molecule-1, 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