Engagement of FcεRI results
in tyrosine phosphorylation of kinases and adaptors, and then an increase in intracellular Ca2 + concentration (27, 28).
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.
In this regard, one of the best models is IFN - stimulated JAK - STAT pathways, in which both STAT1 and STAT2 are activated
by tyrosine phosphorylation in response to IFNs (4).
RESULTS: Short - term treatment of 3T3 - L1 adipocytes with R (+) alpha - lipoic acid rapidly stimulated glucose uptake in a wortmannin - sensitive manner, induced a redistribution of GLUT1 and GLUT4 to the plasma membrane,
caused tyrosine phosphorylation of insulin receptor substrate - 1 and of the insulin receptor, increased the antiphosphotyrosine - associated and insulin receptor substrate - 1 associated phosphatidylinositol 3 - kinase activity and stimulated Akt activity.
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.
TPA / capsaicin cotreatment caused
EGFR tyrosine phosphorylation and activated EGFR downstream signaling, including ERKs and Akt in EGFR / WT, but not EGFR / KO cells.
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.
Importantly, stimulation of the crosslinking of CD4ζ chimeric receptors led to
tyrosine phosphorylation as would be expected for a fully functional chimeric receptor.
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).
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.
Tyrosine phosphorylation sites (yellow circles) promote Eph kinase activity and also provide binding sites for signaling proteins containing SH2 domains.
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.
Hunter's discovery was «the spark that set off a forest fire» of interest in
tyrosine phosphorylation, says Jack Dixon of UC - San Diego.
And not only cancer: «
Tyrosine phosphorylation is now known to be involved in a large number of absolutely crucial cellular functions from normal cell growth to intracellular vesicle trafficking to immune responses.
Depletion of ABL kinases does not affect YAP1 protein abundance, localization, or
tyrosine phosphorylation in breast cancer cells.
Here, we report that signal transducer and activator of transcription (STAT) 2 together with IFN regulatory factor (IRF)-9 can effectively drive the transcription of RIG - G gene by their functional interaction through a STAT1 - independent manner, even without
the tyrosine phosphorylation of STAT2.
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).
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.
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.
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).
EGCG can also mimic insulin by increasing
the tyrosine phosphorylation of both the insulin receptor and insulin receptor substrate - 1 (25)-- the first stage of insulin - stimulated glucose uptake.