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

doi:10.1016/S0014-5793(99)00446-9

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 language	English
Pages (from-to)	77-83
Journal	FEBS Letters
Volume	450
Issue number	1-2
DOIs	https://doi.org/10.1016/S0014-5793(99)00446-9
Publication status	Published - 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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title = "Differential association of cytoplasmic signalling molecules SHP-1, SHP-2, SHIP and phospholipase C-gamma1 with PECAM-1/CD31",

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.",

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",

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

year = "1999",

month = apr,

day = "30",

doi = "10.1016/S0014-5793(99)00446-9",

language = "English",

volume = "450",

pages = "77--83",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "Elsevier",

number = "1-2",

}

TY - JOUR

T1 - Differential association of cytoplasmic signalling molecules SHP-1, SHP-2, SHIP and phospholipase C-gamma1 with PECAM-1/CD31

AU - Pumphrey, N J

AU - Taylor, Vanessa

AU - Freeman, S

AU - Douglas, M R

AU - Bradfield, P F

AU - Young, Stephen

AU - Lord, Janet

AU - Wakelam, M J

AU - Bird, I N

AU - Salmon, M

AU - Buckley, C D

PY - 1999/4/30

Y1 - 1999/4/30

N2 - 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.

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.

KW - Phosphotyrosine

KW - Intracellular Signaling Peptides and Proteins

KW - Humans

KW - Surface Plasmon Resonance

KW - Phosphoric Monoester Hydrolases

KW - Amino Acid Sequence

KW - Protein Tyrosine Phosphatase, Non-Receptor Type 11

KW - Protein Binding

KW - Antigens, CD31

KW - src Homology Domains

KW - Binding Sites

KW - Protein Tyrosine Phosphatases

KW - Phospholipase C gamma

KW - SH2 Domain-Containing Protein Tyrosine Phosphatases

KW - Phosphorylation

KW - Isoenzymes

KW - Molecular Sequence Data

KW - Monocytes

KW - Sequence Homology, Amino Acid

KW - Phosphopeptides

KW - Type C Phospholipases

KW - Vanadates

KW - Signal Transduction

KW - Protein Tyrosine Phosphatase, Non-Receptor Type 6

U2 - 10.1016/S0014-5793(99)00446-9

DO - 10.1016/S0014-5793(99)00446-9

M3 - Article

C2 - 10350061

SN - 0014-5793

VL - 450

SP - 77

EP - 83

JO - FEBS Letters

JF - FEBS Letters

IS - 1-2

ER -

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

Abstract

Keywords

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