Differential association of cytoplasmic signalling molecules SHP-1, SHP-2, SHIP and phospholipase C-gamma1 with PECAM-1/CD31

N J Pumphrey, Vanessa Taylor, S Freeman, M R Douglas, P F Bradfield, Stephen Young, Janet Lord, M J Wakelam, I N Bird, M Salmon, C D Buckley

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Abstract

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 languageEnglish
Pages (from-to)77-83
JournalFEBS Letters
Volume450
Issue number1-2
DOIs
Publication statusPublished - 30 Apr 1999

Keywords

  • Phosphotyrosine
  • Intracellular Signaling Peptides and Proteins
  • Humans
  • Surface Plasmon Resonance
  • Phosphoric Monoester Hydrolases
  • Amino Acid Sequence
  • Protein Tyrosine Phosphatase, Non-Receptor Type 11
  • Protein Binding
  • Antigens, CD31
  • src Homology Domains
  • Binding Sites
  • Protein Tyrosine Phosphatases
  • Phospholipase C gamma
  • SH2 Domain-Containing Protein Tyrosine Phosphatases
  • Phosphorylation
  • Isoenzymes
  • Molecular Sequence Data
  • Monocytes
  • Sequence Homology, Amino Acid
  • Phosphopeptides
  • Type C Phospholipases
  • Vanadates
  • Signal Transduction
  • Protein Tyrosine Phosphatase, Non-Receptor Type 6

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