scholarly journals Overexpression of the Shb SH2 Domain-Protein in Insulin-Producing Cells Leads to Altered Signaling Through the IRS-1 and IRS-2 Proteins

2002 ◽  
Vol 8 (11) ◽  
pp. 695-704 ◽  
Author(s):  
Nils Welsh ◽  
Natalia Makeeva ◽  
Michael Welsh
Keyword(s):  
Sh2 Domain ◽  
Insulin Producing Cells ◽  
Domain Protein

Probing factors affecting the gas phase stabilities of noncovalent complexes formed by peptides bound to the Grb2 SH2 domain protein

2004 ◽  
Vol 6 (10) ◽  
pp. 2572 ◽  
Author(s):  
M. Isabel Catalina ◽  
Nico J. de Mol ◽  
Marcel J. E. Fischer ◽  
Albert J. R. Heck
Keyword(s):  
Gas Phase ◽  
Sh2 Domain ◽  
Noncovalent Complexes ◽  
Factors Affecting ◽  
Domain Protein

scholarly journals Calcium Release at Fertilization in Starfish Eggs Is Mediated by Phospholipase Cγ

1997 ◽  
Vol 138 (6) ◽  
pp. 1303-1311 ◽  
Author(s):  
David J. Carroll ◽  
Chodavarapu S. Ramarao ◽  
Lisa M. Mehlmann ◽  
Serge Roche ◽  
Mark Terasaki ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Calcium Release ◽  
Specific Inhibitor ◽  
Sh2 Domain ◽  
High Concentration ◽  
Serotonin 2C Receptor ◽  
Sh2 Domains ◽  
Src Homology 2 ◽  
Src Homology ◽  
Domain Protein

Although inositol trisphosphate (IP3) functions in releasing Ca2+ in eggs at fertilization, it is not known how fertilization activates the phospholipase C that produces IP3. To distinguish between a role for PLCγ, which is activated when its two src homology-2 (SH2) domains bind to an activated tyrosine kinase, and PLCβ, which is activated by a G protein, we injected starfish eggs with a PLCγ SH2 domain fusion protein that inhibits activation of PLCγ. In these eggs, Ca2+ release at fertilization was delayed, or with a high concentration of protein and a low concentration of sperm, completely inhibited. The PLCγSH2 protein is a specific inhibitor of PLCγ in the egg, since it did not inhibit PLCβ activation of Ca2+ release initiated by the serotonin 2c receptor, or activation of Ca2+ release by IP3 injection. Furthermore, injection of a PLCγ SH2 domain protein mutated at its phosphotyrosine binding site, or the SH2 domains of another protein (the phosphatase SHP2), did not inhibit Ca2+ release at fertilization. These results indicate that during fertilization of starfish eggs, activation of phospholipase Cγ by an SH2 domain-mediated process stimulates the production of IP3 that causes intracellular Ca2+ release.

scholarly journals The phosphotyrosine interaction domain of Shc binds an LXNPXY motif on the epidermal growth factor receptor.

1995 ◽  
Vol 15 (8) ◽  
pp. 4403-4409 ◽  
Author(s):  
A G Batzer ◽  
P Blaikie ◽  
K Nelson ◽  
J Schlessinger ◽  
B Margolis
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Growth Factor Receptor ◽  
Sh2 Domain ◽  
Interaction Domain ◽  
Competition Analysis ◽  
Amino Terminal ◽  
Epidermal Growth ◽  
Domain Protein

Shc is an SH2 domain protein that is tyrosine phosphorylated in cells stimulated with a variety of growth factors and cytokines. Once phosphorylated, Shc binds the Grb2-Sos complex, leading to Ras activation. Shc can interact with tyrosine-phosphorylated proteins by binding to phosphotyrosine in the context of an NPXpY motif, where pY is a phosphotyrosine. This is an unusual binding site for an SH2 domain protein whose binding specificity is usually controlled by residues carboxy terminal, not amino terminal, to the phosphotyrosine. Recently we identified a second region in Shc, named the phosphotyrosine interaction (PI) domain, and we have found it to be present in a variety of other cellular proteins. In this study we used a dephosphorylation protection assay, competition analysis with phosphotyrosine-containing synthetic peptides, and epidermal growth factor receptor (EGFR) mutants to determine the binding sites of the PI domain of Shc on the EGFR. We demonstrate that the PI domain of Shc binds the LXNPXpY motif that encompasses Y-1148 of the activated EGFR. We conclude that the PI domain imparts to Shc its ability to bind the NPXpY motif.

scholarly journals The SH2 domain protein Shep1 regulates the in vivo signaling function of the scaffolding protein Cas

2010 ◽  
Vol 22 (11) ◽  
pp. 1745-1752 ◽  
Author(s):  
Séverine Roselli ◽  
Yann Wallez ◽  
Lei Wang ◽  
Virginie Vervoort ◽  
Elena B. Pasquale
Keyword(s):  
Sh2 Domain ◽  
Scaffolding Protein ◽  
Signaling Function ◽  
Domain Protein
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