During the development of blood cells it is activated by
tyrosine phosphorylation and can switch certain genes on or off.
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.
Samelson LE, Patel MD, Weissman AM, Harford JB, Klausner RD. Antigen activation of murine T cells induces
tyrosine phosphorylation of a polypeptide associated with the T cell antigen receptor.
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.
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.
(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.
The SDF - 1 / CXCR4 interaction stimulates
tyrosine phosphorylation of CXCR4, followed by the activation of multiple G protein - dependent signaling pathways, which may be different among cell types.
Effects of
tyrosine phosphorylation of cortactin on podosome formation in A7r5 vascular smooth muscle cells.
Importantly, stimulation of the crosslinking of CD4ζ chimeric receptors led to
tyrosine phosphorylation as would be expected for a fully functional chimeric receptor.
Hunter is known for his 1979 discovery of a mechanism called
tyrosine phosphorylation, which is a molecular switch that turns normal cells cancerous.
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).
Recently, accumulating observations support the notion that STAT proteins can drive gene expression without
tyrosine phosphorylation (14 — 19).
Similarly, increased level of STAT2
tyrosine phosphorylation was detected as well in IRF - 1 — transfected HT1080 cells (Fig. 4B).
Accordingly, IL - 4 can specifically induce
tyrosine phosphorylation of STAT6.
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 phosphorylation.
Cell type - specific and
tyrosine phosphorylation - independent nuclear presence of STAT1 and STAT3.
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.
Requirement of
tyrosine phosphorylation for rapid activation of a DNA binding factor by IL - 4.
Toxoplasma Rhoptry Protein 16 (ROP16) Subverts Host Function by Direct
Tyrosine Phosphorylation of STAT6
Interferons induce
tyrosine phosphorylation of the eIF2 -LCB- alpha -RCB- kinase PKR through activation of Jak1 and Tyk2
Engagement of FcεRI results in
tyrosine phosphorylation of kinases and adaptors, and then an increase in intracellular Ca2 + concentration (27, 28).
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.
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.
Not exact matches
C - Terminal
Tyrosine Residue Modifications Modulate the Protective
Phosphorylation of Serine 129 of α - Synuclein in a Yeast Model of Parkinson's Disease.
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.
The most common mechanism for constitutive activation and
phosphorylation of STAT factors is the dysregulation of
tyrosine kinases.
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).
We have identified
tyrosine and serine / threonine
phosphorylation sites of Eph receptors and ephrins using mass spectrometry and investigated the signaling role of these
phosphorylation sites.
RIPK2 is activated via
tyrosine (Y)(pY474) and serine (S)(pS176)
phosphorylation and ubiquitination events to allow for associations with downstream components.
RIPK2 inhibitor 1 inhibits
phosphorylation at serine 176 and
tyrosine 474 and possible inhibition of ubiquitination of RIPK2.
Zinc is involved in insulin signaling by inhibiting the enzyme protein
tyrosine phosphatase to increase
phosphorylation of the insulin receptor.