Differential association of cytoplasmic signalling molecules SHP-1, SHP-2, SHIP and phospholipase C-gamma1 with PECAM-1/CD31 (Q28144872)

ORCID Public Data File 2021

Christopher D Buckley

1 reference

ORCID Public Data File 2021

author name string

N J Pumphrey

1

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V Taylor

2

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M R Douglas

4

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P F Bradfield

5

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S P Young

6

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J M Lord

7

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M J Wakelam

8

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I N Bird

9

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M Salmon

10

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C D Buckley

11

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language of work or name

English

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publication date

30 April 1999

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published in

FEBS Letters

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volume

450

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page(s)

77-83

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issue

1-2

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cites work

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Characterization of phosphotyrosine binding motifs in the cytoplasmic domain of platelet/endothelial cell adhesion molecule-1 (PECAM-1) that are required for the cellular association and activation of the protein-tyrosine phosphatase, SHP-2

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The protein-tyrosine phosphatase SHP-2 associates with tyrosine-phosphorylated adhesion molecule PECAM-1 (CD31)

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Platelet endothelial cell adhesion molecule-1 is phosphorylatable by c-Src, binds Src-Src homology 2 domain, and exhibits immunoreceptor tyrosine-based activation motif-like properties

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Integrin engagement mediates tyrosine dephosphorylation on platelet-endothelial cell adhesion molecule 1.

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Ligation of CD31/PECAM-1 modulates the function of lymphocytes, monocytes and neutrophils.

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Definition of the sites of interaction between the protein tyrosine phosphatase SHP-1 and CD22

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The 64-kDa protein that associates with the platelet-derived growth factor receptor beta subunit via Tyr-1009 is the SH2-containing phosphotyrosine phosphatase Syp

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SH2 domains recognize specific phosphopeptide sequences

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Engagement of human PECAM-1 (CD31) on human endothelial cells increases intracellular calcium ion concentration and stimulates prostacyclin release

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CD31 expressed on distinctive T cell subsets is a preferential amplifier of beta 1 integrin-mediated adhesion

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Integrins and inside-out signal transduction: converging signals from PKC and PIP3.

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Inhibitory receptors abound?

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Association of tyrosine phosphatases SHP-1 and SHP-2, inositol 5-phosphatase SHIP with gp49B1, and chromosomal assignment of the gene

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Tyrosine phosphorylation and relocation of SHIP are integrin-mediated in thrombin-stimulated human blood platelets

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Activation-dependent changes in human platelet PECAM-1: phosphorylation, cytoskeletal association, and surface membrane redistribution

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Switched at birth: a new family for PECAM-1.

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The T cell receptor/CD3 complex is composed of at least two autonomous transduction modules.

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Tyrosine Phosphorylation of Platelet Endothelial Cell Adhesion Molecule-1 Induced by Lysophosphatidylcholine in Cultured Endothelial Cells

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The negative signaling molecule SH2 domain-containing inositol-polyphosphate 5-phosphatase (SHIP) binds to the tyrosine-phosphorylated beta subunit of the high affinity IgE receptor

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