PMID- 10350061
OWN - NLM
STAT- MEDLINE
DCOM- 19990624
LR  - 20190621
IS  - 0014-5793 (Print)
IS  - 0014-5793 (Linking)
VI  - 450
IP  - 1-2
DP  - 1999 Apr 30
TI  - Differential association of cytoplasmic signalling molecules SHP-1, SHP-2, SHIP
      and phospholipase C-gamma1 with PECAM-1/CD31.
PG  - 77-83
AB  - 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.
FAU - Pumphrey, N J
AU  - Pumphrey NJ
AD  - Division of Immunity and Infection, University of Birmingham, UK.
FAU - Taylor, V
AU  - Taylor V
FAU - Freeman, S
AU  - Freeman S
FAU - Douglas, M R
AU  - Douglas MR
FAU - Bradfield, P F
AU  - Bradfield PF
FAU - Young, S P
AU  - Young SP
FAU - Lord, J M
AU  - Lord JM
FAU - Wakelam, M J
AU  - Wakelam MJ
FAU - Bird, I N
AU  - Bird IN
FAU - Salmon, M
AU  - Salmon M
FAU - Buckley, C D
AU  - Buckley CD
LA  - eng
GR  - Wellcome Trust/United Kingdom
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - FEBS Lett
JT  - FEBS letters
JID - 0155157
RN  - 0 (Intracellular Signaling Peptides and Proteins)
RN  - 0 (Isoenzymes)
RN  - 0 (Phosphopeptides)
RN  - 0 (Platelet Endothelial Cell Adhesion Molecule-1)
RN  - 0 (pervanadate)
RN  - 21820-51-9 (Phosphotyrosine)
RN  - 3WHH0066W5 (Vanadates)
RN  - EC 3.1.3.2 (Phosphoric Monoester Hydrolases)
RN  - EC 3.1.3.48 (PTPN11 protein, human)
RN  - EC 3.1.3.48 (PTPN6 protein, human)
RN  - EC 3.1.3.48 (Protein Tyrosine Phosphatase, Non-Receptor Type 11)
RN  - EC 3.1.3.48 (Protein Tyrosine Phosphatase, Non-Receptor Type 6)
RN  - EC 3.1.3.48 (Protein Tyrosine Phosphatases)
RN  - EC 3.1.3.48 (SH2 Domain-Containing Protein Tyrosine Phosphatases)
RN  - EC 3.1.3.86 (INPPL1 protein, human)
RN  - EC 3.1.3.86 (Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases)
RN  - EC 3.1.4.- (Type C Phospholipases)
RN  - EC 3.1.4.3 (Phospholipase C gamma)
SB  - IM
MH  - Amino Acid Sequence
MH  - Binding Sites
MH  - Humans
MH  - Intracellular Signaling Peptides and Proteins
MH  - Isoenzymes/*metabolism
MH  - Molecular Sequence Data
MH  - Monocytes/metabolism
MH  - Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases
MH  - Phospholipase C gamma
MH  - Phosphopeptides/metabolism
MH  - Phosphoric Monoester Hydrolases/*metabolism
MH  - Phosphorylation
MH  - Phosphotyrosine/metabolism
MH  - Platelet Endothelial Cell Adhesion Molecule-1/chemistry/*metabolism
MH  - Protein Binding
MH  - Protein Tyrosine Phosphatase, Non-Receptor Type 11
MH  - Protein Tyrosine Phosphatase, Non-Receptor Type 6
MH  - Protein Tyrosine Phosphatases/*metabolism
MH  - SH2 Domain-Containing Protein Tyrosine Phosphatases
MH  - Sequence Homology, Amino Acid
MH  - Signal Transduction
MH  - Surface Plasmon Resonance
MH  - Type C Phospholipases/*metabolism
MH  - Vanadates/pharmacology
MH  - src Homology Domains
EDAT- 1999/06/01 00:00
MHDA- 1999/06/01 00:01
CRDT- 1999/06/01 00:00
PHST- 1999/06/01 00:00 [pubmed]
PHST- 1999/06/01 00:01 [medline]
PHST- 1999/06/01 00:00 [entrez]
AID - S0014-5793(99)00446-9 [pii]
AID - 10.1016/s0014-5793(99)00446-9 [doi]
PST - ppublish
SO  - FEBS Lett. 1999 Apr 30;450(1-2):77-83. doi: 10.1016/s0014-5793(99)00446-9.