The phosphotyrosine phosphatase SHP-2 participates in a multimeric signaling complex and regulates T cell receptor (TCR) coupling to the Ras/mitogen-activated protein kinase (MAPK) pathway in Jurkat T cells (Q42971603)

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scientific article published on May 1998

Language	Label	Description	Also known as
English	The phosphotyrosine phosphatase SHP-2 participates in a multimeric signaling complex and regulates T cell receptor (TCR) coupling to the Ras/mitogen-activated protein kinase (MAPK) pathway in Jurkat T cells	scientific article published on May 1998

Statements

scholarly article

1 reference

Europe PubMed Central

PMC publication ID

12 November 2017

The phosphotyrosine phosphatase SHP-2 participates in a multimeric signaling complex and regulates T cell receptor (TCR) coupling to the Ras/mitogen-activated protein kinase (MAPK) pathway in Jurkat T cells (English)

1 reference

Europe PubMed Central

PMC publication ID

12 November 2017

author name string

J A Frearson

1

1 reference

Europe PubMed Central

PMC publication ID

12 November 2017

D R Alexander

2

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Europe PubMed Central

PMC publication ID

12 November 2017

language of work or name

0 references

publication date

1 May 1998

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Europe PubMed Central

PMC publication ID

12 November 2017

Journal of Experimental Medicine

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Europe PubMed Central

PMC publication ID

12 November 2017

187

1 reference

Europe PubMed Central

PMC publication ID

12 November 2017

9

1 reference

Europe PubMed Central

PMC publication ID

12 November 2017

1417-1426

1 reference

Europe PubMed Central

PMC publication ID

12 November 2017

LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation

1 reference

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Coupling of Ras and Rac Guanosine Triphosphatases Through the Ras Exchanger Sos

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Role of Substrates and Products of PI 3-kinase in Regulating Activation of Rac-Related Guanosine Triphosphatases by Vav

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Aberrant TCR-mediated signaling in CD45-null thymocytes involves dysfunctional regulation of Lck, Fyn, TCR-zeta, and ZAP-70.

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The role of phosphotyrosine phosphatases in haematopoietic cell signal transduction

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p95vav associates with tyrosine-phosphorylated SLP-76 in antigen-stimulated T cells

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A family of proteins that inhibit signalling through tyrosine kinase receptors

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A novel membrane glycoprotein, SHPS-1, that binds the SH2-domain-containing protein tyrosine phosphatase SHP-2 in response to mitogens and cell adhesion

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Lack of SHPTP1 results in src-family kinase hyperactivation and thymocyte hyperresponsiveness

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T cell antigen receptor signal transduction pathways

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The SH2 domain-containing tyrosine phosphatase PTP1D is required for interferon alpha/beta-induced gene expression

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Expression of dominant negative mutant SHPTP2 attenuates phosphatidylinositol 3'-kinase activity via modulation of phosphorylation of insulin receptor substrate-1.

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Lck regulates the tyrosine phosphorylation of the T cell receptor subunits and ZAP-70 in murine thymocytes

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Direct regulation of ZAP-70 by SHP-1 in T cell antigen receptor signaling

1 reference

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Multiple requirements for SHPTP2 in epidermal growth factor-mediated cell cycle progression

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A Grb2-associated docking protein in EGF- and insulin-receptor signalling

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Differential functions of the two Src homology 2 domains in protein tyrosine phosphatase SH-PTP1

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CD45 specifically modulates binding of Lck to a phosphopeptide encompassing the negative regulatory tyrosine of Lck.

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SH3 domains of the adapter molecule Grb2 complex with two proteins in T cells: the guanine nucleotide exchange protein Sos and a 75-kDa protein that is a substrate for T cell antigen receptor-activated tyrosine kinases

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Expression of catalytically inactive Syp phosphatase in 3T3 cells blocks stimulation of mitogen-activated protein kinase by insulin.

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Phosphatidylinositol-3-OH kinase as a direct target of Ras

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Raf meets Ras: completing the framework of a signal transduction pathway

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The role of protein tyrosine kinases and protein tyrosine phosphatases in T cell antigen receptor signal transduction

1 reference

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Role of SH-PTP2, a protein-tyrosine phosphatase with Src homology 2 domains, in insulin-stimulated Ras activation

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Altered expression of protein-tyrosine phosphatase 2C in 293 cells affects protein tyrosine phosphorylation and mitogen-activated protein kinase activation

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"Viable motheaten," a new allele at the motheaten locus. I. Pathology

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Structure of the insulin receptor substrate IRS-1 defines a unique signal transduction protein

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1 reference

https://pubmed.ncbi.nlm.nih.gov/9565634

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/9565634

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Characterization of a novel tyrosine phosphorylated 100-kDa protein that binds to SHP-2 and phosphatidylinositol 3'-kinase in myeloid cells

1 reference

https://pubmed.ncbi.nlm.nih.gov/9565634

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The SH2-containing protein-tyrosine phosphatase SH-PTP2 is required upstream of MAP kinase for early Xenopus development

1 reference

https://pubmed.ncbi.nlm.nih.gov/9565634

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1084/JEM.187.9.1417

1 reference

Europe PubMed Central

PMC publication ID

12 November 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

12 November 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

12 November 2017

ResearchGate publication ID

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