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.
Engagement of FcεRI results in
tyrosine phosphorylation of kinases and adaptors, and then an increase in intracellular Ca2 + concentration (27, 28).
Interferons induce
tyrosine phosphorylation of the eIF2 -LCB- alpha -RCB- kinase PKR through activation of Jak1 and Tyk2
Toxoplasma Rhoptry Protein 16 (ROP16) Subverts Host Function by Direct
Tyrosine Phosphorylation of STAT6
Accordingly, IL - 4 can specifically induce
tyrosine phosphorylation of STAT6.
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).
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).
Effects of
tyrosine phosphorylation of cortactin on podosome formation in A7r5 vascular smooth muscle cells.
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.
Fyn membrane localization is necessary to induce the constitutive
tyrosine phosphorylation of Sam68 in the nucleus of T lymphocytes.
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.
At a molecular level, loss of insulin signaling in astrocytes impaired
tyrosine phosphorylation of Munc18c.
Not exact matches
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.
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.
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.
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 most common mechanism for constitutive activation and
phosphorylation of STAT factors is the dysregulation
of tyrosine kinases.
Similarly, increased level
of STAT2
tyrosine phosphorylation was detected as well in IRF - 1 — transfected HT1080 cells (Fig. 4B).
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.
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.
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).
RIPK2 inhibitor 1 inhibits
phosphorylation at serine 176 and
tyrosine 474 and possible inhibition
of ubiquitination
of RIPK2.
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.
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.