Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

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.

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