(Q24315098)

English

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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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 (English)

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1 reference

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author name string

D E Jackson

1

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K R Kupcho

2

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P J Newman

3

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language of work or name

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publication date

3 October 1997

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Journal of Biological Chemistry

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272

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24868-75

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40

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A noncatalytic domain conserved among cytoplasmic protein-tyrosine kinases modifies the kinase function and transforming activity of Fujinami sarcoma virus P130gag-fps

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A novel viral oncogene with structural similarity to phospholipase C

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Molecular cloning and expression of the major protein kinase C substrate of platelets

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SH2 domains recognize specific phosphopeptide sequences

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Protein modules and signalling networks

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SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins

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Analysis of the binding of the Src homology 2 domain of Csk to tyrosine-phosphorylated proteins in the suppression and mitotic activation of c-Src

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PECAM-1 (CD31) Cloning and Relation to Adhesion Molecules of the Immunoglobulin Gene Superfamily

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EndoCAM: a novel endothelial cell-cell adhesion molecule

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The role of PECAM-1 in vascular cell biology

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The biology of PECAM-1.

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Individually distinct Ig homology domains in PECAM-1 regulate homophilic binding and modulate receptor affinity

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Platelet endothelial cell adhesion molecule-1 (PECAM-1) homophilic adhesion is mediated by immunoglobulin-like domains 1 and 2 and depends on the cytoplasmic domain and the level of surface expression

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PECAM-1 is required for transendothelial migration of leukocytes

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CD31/PECAM-1-driven chemokine-independent transmigration of human T lymphocytes.

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Soluble domain 1 of platelet-endothelial cell adhesion molecule (PECAM) is sufficient to block transendothelial migration in vitro and in vivo

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Platelet endothelial cell adhesion molecule, PECAM-1, modulates cell migration

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Thrombospondin-1, a natural inhibitor of angiogenesis, regulates platelet-endothelial cell adhesion molecule-1 expression and endothelial cell morphogenesis

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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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Murine platelet endothelial cell adhesion molecule (PECAM-1)/CD31 modulates beta 2 integrins on lymphokine-activated killer cells

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Aggregation of the high affinity IgE receptor results in the tyrosine phosphorylation of the surface adhesion protein PECAM-1 (CD31)

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Tyrosine phosphorylation of P-selectin in intact platelets and in a disulphide-linked complex with immunoprecipitated pp60c-src

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Identification of a human src homology 2-containing protein-tyrosine-phosphatase: a putative homolog of Drosophila corkscrew

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A widely expressed human protein-tyrosine phosphatase containing src homology 2 domains

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SH2-containing phosphotyrosine phosphatase as a target of protein-tyrosine kinases

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Activation of a phosphotyrosine phosphatase by tyrosine phosphorylation

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Choice of STATs and other substrates specified by modular tyrosine-based motifs in cytokine receptors

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Protein-tyrosine-phosphatase SHPTP2 couples platelet-derived growth factor receptor beta to Ras

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A new function for a phosphotyrosine phosphatase: linking GRB2-Sos to a receptor tyrosine kinase

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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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Spatial constraints on the recognition of phosphoproteins by the tandem SH2 domains of the phosphatase SH-PTP2

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Molecular basis for interaction of the protein tyrosine kinase ZAP-70 with the T-cell receptor

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Activation of protein-tyrosine phosphatase SH-PTP2 by a tyrosine-based activation motif of a novel brain molecule

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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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Direct determination of the sequence recognition requirements of the SH2 domains of SH-PTP2

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Tyrosines 1021 and 1009 are phosphorylation sites in the carboxy terminus of the platelet-derived growth factor receptor beta subunit and are required for binding of phospholipase C gamma and a 64-kilodalton protein, respectively

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Monocyte-selective transendothelial migration: dissection of the binding and transmigration phases by an in vitro assay

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Potent stimulation of SH-PTP2 phosphatase activity by simultaneous occupancy of both SH2 domains

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Both SH2 domains are involved in interaction of SHP-1 with the epidermal growth factor receptor but cannot confer receptor-directed activity to SHP-1/SHP-2 chimera

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Identifiers

10.1074/JBC.272.40.24868

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