Sentences with phrase «in tyrosine phosphorylation»

Engagement of FcεRI results in tyrosine phosphorylation of kinases and adaptors, and then an increase in intracellular Ca2 + concentration (27, 28).

Specifically, they are interested in those genes that are involved in tyrosine phosphorylation — the attachment of a phosphate group (a phosphorous surrounded by oxygen atoms) to distinct sites in protein chains where there is a tyrosine residue.

Not exact matches

The sequence similarity between MAD - 3 and pp40 includes a casein kinase II and consensus tyrosine phosphorylation site, as well as five repeats of a sequence found in the human erythrocyte protein ankyrin.

At a molecular level, loss of insulin signaling in astrocytes impaired tyrosine phosphorylation of Munc18c.

Zhang, Y. and Wolf - Yadlin, A. and Ross, P. L. and Pappin, D. J. and Rush, J. and Lauffenburger, D. A. and White, F. M. (2005) Time - resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules.

(e, g) Western blot (WB) analysis of tyrosine phosphorylation (pTyr) and total Tie2 after Tie2 immunoprecipitation (IP) in BP (e) and HUVEC (g) upon stimulation with recombinant human (rh) Ang1 compared to unstimulated (us) cells.

Fyn membrane localization is necessary to induce the constitutive tyrosine phosphorylation of Sam68 in the nucleus of T lymphocytes.

C - Terminal Tyrosine Residue Modifications Modulate the Protective Phosphorylation of Serine 129 of α - Synuclein in a Yeast Model of Parkinson's Disease.

Effects of tyrosine phosphorylation of cortactin on podosome formation in A7r5 vascular smooth muscle cells.

Tyrosine is an amino acid present in proteins that contains a hydroxyl moiety, and kinases are enzymes that catalyze phosphorylation (addition of a phosphate group) of various substrates in the cell.

Depletion of ABL kinases does not affect YAP1 protein abundance, localization, or tyrosine phosphorylation in breast cancer cells.

During the past decade, data on the putative roles of STAT proteins in mediating gene expression without tyrosine phosphorylation have been accumulating.

The results revealed that the supernatant of 72 - hour ATRA - treated NB4 cells was sufficient to induce the tyrosine phosphorylation of STAT2 and the endogenous RIG - G level in U3A cells, in comparison with the relative consistent level of total STAT2 (Fig. 3B).

Unlike IFNα - activated ISGF3 complex in which tyrosine - phosphorylated STAT proteins are required, IRF - 9 could successfully interact with either wt STAT2 or mutant STAT2 - Y690F in the absence of IFNα, although the interaction between IRF - 9 and wt STAT2 could be obviously enhanced by IFNα via tyrosine phosphorylation of STAT2 (Fig. 2A).

Similarly, increased level of STAT2 tyrosine phosphorylation was detected as well in IRF - 1 — transfected HT1080 cells (Fig. 4B).

To exclude this possibility, we constructed a phosphorylation - deficient STAT6 mutant in which the potential phosphorylated tyrosine at position 641 was mutated to a tryptophan (STAT6Y641W).

In this study, we provide the first evidence that in STAT1 - deficient U3A cells, STAT2 forms a complex with IRF - 9 on the ISRE regions of RIG - G promoter and effectively mediates the transcription of RIG - G gene, even without the tyrosine phosphorylatioIn this study, we provide the first evidence that in STAT1 - deficient U3A cells, STAT2 forms a complex with IRF - 9 on the ISRE regions of RIG - G promoter and effectively mediates the transcription of RIG - G gene, even without the tyrosine phosphorylatioin STAT1 - deficient U3A cells, STAT2 forms a complex with IRF - 9 on the ISRE regions of RIG - G promoter and effectively mediates the transcription of RIG - G gene, even without the tyrosine phosphorylation.

The idea that both STAT2 and IRF - 9 were basic components necessary for RIG - G expression was also supported by the fact that ATRA could not only induce the total amounts of STAT2 and IRF - 9 proteins but also increase the tyrosine phosphorylation level of STAT2 in NB4 cells (Fig. 1A).

Here, we have shown for the first time that the unphosphorylated STAT2 could play an important role in RIG - G gene expression by interacting with IRF - 9, further reinforcing the idea that STAT proteins could function as transcription factors in the absence of tyrosine phosphorylation.

For example, our past work showed that two conserved tyrosine phosphorylation sites in the juxtamembrane segment of the Eph receptors not only mediate association with binding partners but also regulate receptor kinase activity.

Twelve - hour exposure of 3T3 - L1 adipocytes to H (2) O (2) or TNF - alpha resulted in the increase of c - Jun NH (2)- terminal kinase (JNK) activation and insulin receptor substrate 1 (IRS1) serine 307 phosphorylation, concomitantly with the decrease in insulin - stimulated IRS1 tyrosine phosphorylation and cellular glucose uptake.

Zinc is involved in insulin signaling by inhibiting the enzyme protein tyrosine phosphatase to increase phosphorylation of the insulin receptor.

METHODS: We treated 3T3 - L1 adipocytes with 2.5 mmol / l R (+) alpha - lipoic acid for 2 to 60 min, followed by assays of: 2 - deoxyglucose uptake; glucose transporter 1 and 4 (GLUT1 and GLUT4) subcellular localization; tyrosine phosphorylation of the insulin receptor or of the insulin receptor substrate - 1 in cell lysates; association of phosphatidylinositol 3 - kinase activity with immunoprecipitates of proteins containing phosphotyrosine or of insulin receptor substrate - 1 using a in vitro kinase assay; association of the p85 subunit of phosphatidylinositol 3 - kinase with phosphotyrosine proteins or with insulin receptor substrate - 1; and in vitro activity of immunoprecipitated Akt1.