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Target |
Regulator |
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| Kung et al. (1989) | IL-2 | | T cell | There was no difference in biological activity between non-phosphorylated and phosphorylated IL-2, as determined by a T cell growth assay. |
| Asao et al. (1990) | IL-2Rp75 | | T cells | The present study using TU11 mAb demonstrates the IL-2-induced phosphorylation of IL-2Rp75 on tyrosine residues in IL-2-dependent T cells. |
| Evans et al. (1992) | Interleukin-2 | | T-cells | Interleukin-2-dependent phosphorylation of the retinoblastoma-susceptibility-gene product p110-115RB in human T-cells.
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| Paliogianni et al. (1993) | IL-2-dependent | | T cell | Inhibition of T cell proliferation by Dex was associated with decreased IL-2-dependent tyrosine phosphorylation of several intracellular proteins and decreased phosphorylation of the retinoblastoma gene product Rb, a protein essential for controlling the progression of cells through the cell cycle. |
| Ogawa et al. (1987) | interleukin 2 | | T cell | Tyrosine phosphorylation of an interleukin 2 receptor-like protein in cells transformed by human T cell leukemia virus type I.
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| Lanier et al. (1988) | IL-2 | | T lymphocytes | In this study, we describe an activation antigen, Leu-23, that is rapidly induced and phosphorylated after IL-2 stimulation of NK cells and a subset of low buoyant density T lymphocytes. |
| Brockdorff et al. (2001) | IL-2 | | T cells | Preincubation of cells with the Src family kinase inhibitor, PP1, surprisingly increased the IL-2- and IL-15-induced tyrosine phosphorylation of Gab2, indicating that an Src family kinase member negatively regulates IL-2 receptor signaling in MF T cells. |
| Goebel et al. (2001) | IL-2 | | T lymphocytes | RESULTS: In human T lymphocytes, 16H5 attenuated both the tyrosine phosphorylation of STAT5 by IL-2 and the IL-2-induced DNA-binding of this transcription factor. |
| Kabelitz (2010) | IL-2 | | T cells | T cells (by N-BP or phosphoantigen plus IL-2) followed by the adoptive transfer of in vitro expanded ?? |
| Shackelford and Trowbridge (1986) | IL-2 | | T lymphocytes | IL-2 receptors on normal human T lymphocytes and the leukemic cell line, HUT102B2, are rapidly phosphorylated in vivo in response to the tumor-promoting phorbol ester, 12-O-tetradecanoylphorbol 13-acetate (TPA). |
| Farrar and Ferris (1989) | IL 2 | | T lymphocytes | Here, using anti-phosphotyrosine antibodies to purify phosphotyrosyl proteins and two-dimensional gel analysis, we show that IL 2 stimulates rapid tyrosine phosphorylation of a variety of cellular proteins, including pp180, pp92, and pp42 in activated human T lymphocytes. |
| Ishii et al. (1987) | interleukin 2 | | T-cells | Characterization of interleukin 2-stimulated phosphorylation of 67 and 63 kDa proteins in human T-cells.
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| Ishii et al. (1987) | interleukin 2 | | T-cell | We have investigated rapid and marked phosphorylation of cellular proteins induced by interleukin 2 (IL-2) in both phytohaemagglutinin-stimulated normal peripheral blood leucocytes, and IL-2-dependent or -independent human T-cell lines bearing human T-cell leukaemia (lymphotropic) virus type I. |
| Leonard et al. (1985) | TCGF | | T-cells | Lastly, we demonstrate that at least some TCGF receptors are phosphorylated and sulfated, and that TCGF receptors on phytohemagglutinin-activated normal T-cells are more heavily sulfated than those on HUT-102B2 cells.
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| Song et al. (1993) | IL-2 | | T cells | In this study, the relationship between IL-2 production and the protein tyrosine phosphorylation pattern of human Jurkat T cells was investigated using phosphotyrosine immunoblotting analysis. |
| Adamson et al. (1999) | IL-2 | | T lymphocyte | ICAM-1-stimulated tyrosine phosphorylation of the actin-associated molecule cortactin and ICAM-1-mediated, Ag/IL-2-stimulated T lymphocyte migration through EC monolayers were inhibited following pretreatment of EC with cytochalasin D. |
| Lafont et al. (1998) | IL2 | | T cell | Moreover, activation of this pathway appeared to be essential, since its blockade by a specific inhibitor of the MEK-1 kinase abolished IL2 gene transcription; in contrast, in T cells stimulated with phytohemagglutinin M(PHA), another potent T cell mitogenic lectin, blockade of MEK-1 reduced but did not totally inhibit either ERK-2 phosphorylation or IL2 mRNA expression. |
| Kirken et al. (1997) | IL2 | | T lymphocytes | We now report that IL2 stimulated marked phosphorylation of serine and tyrosine residues of both Stat5a and Stat5b in human T lymphocytes and in several IL2-responsive lymphocytic cell lines. |
| Migone et al. (2001) | IL-2-induced | | T cells | The results of this study show that DUB-2 is expressed in human T-cell lymphotropic virus-I (HTLV-1)-transformed T cells that exhibit constitutive activation of the IL-2 JAK/STAT (signal transducers and activators of transcription) pathway, and when expressed in Ba/F3 cells DUB-2 markedly prolonged IL-2-induced STAT5 phosphorylation. |
| Tao et al. (1996) | IL-2 gene | | T cell | These results have localized the effect of T2 to a step in the T cell activation cascade after initial second messenger generation, tyrosine phosphorylation and protein kinase activation, but before IL-2 gene transcription.
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| Brockdorff et al. (2001) | interleukin-2 | | T cells | Gab2 is phosphorylated on tyrosine upon interleukin-2/interleukin-15 stimulation in mycosis-fungoides-derived tumor T cells and associates inducibly with SHP-2 and Stat5a.
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| Nielsen et al. (1994) | Interleukin-2 | | T lymphocytes | Interleukin-2 induces tyrosine phosphorylation and nuclear translocation of stat3 in human T lymphocytes.
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| Adachi et al. (1997) | IL-2-dependent | | T-cell | Furthermore, the IL-2 stimulation also induced tyrosine phosphorylation of SHP-2 in the human IL-2-dependent T-cell line ILT-Mat. |
| Forrest et al. (2005) | IL-2-induced | | T cells | However, T cells studied post-transplant neither exhibited CD25 or -122 upregulation nor IL-2-induced tyrosine phosphorylation events, indicating broad, persistent suppression of the IL-2R signaling machinery which thus appears largely inaccessible for Dac in actual transplant recipients. |
| Vandenberghe et al. (1992) | IL-2 | | T cells | Herbimycin A, a protein tyrosine kinase inhibitor, could prevent CD28-induced tyrosine phosphorylation and CD28-induced IL-2 production in normal T cells. |
| O'Gorman et al. (2009) | IL-2-dependent | | T cell | Within hours of T cell priming, IL-2-dependent STAT5 phosphorylation occurred primarily in Foxp3(+) regulatory T cells. |
| Craddock et al. (2007) | IL-2 | | T cell | Lower T cell proliferation in schizophrenia patients was not found to result from deficient early tyrosine phosphorylation signalling or lower IL-2 (interleukin-2) production, as these parameters were similar between patients and controls, as was the expression of CD25, the IL-2 receptor alpha chain. |
| Zhu et al. (1994) | Interleukin-2 | | T cell | Interleukin-2-induced tyrosine phosphorylation of Shc proteins correlates with factor-dependent T cell proliferation.
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| Zmuidzinas et al. (1991) | Interleukin-2-triggered | | T cells | Interleukin-2-triggered Raf-1 expression, phosphorylation, and associated kinase activity increase through G1 and S in CD3-stimulated primary human T cells.
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| Vij et al. (2008) | IL2 | | T cells | The expression of SOCS3 is rapidly induced in T cells in response to IL2 and can strongly inhibit IL2-induced STAT5 phosphorylation [11]. |
| Piau et al. (1989) | Interleukin 2 | | T cell | Interleukin 2 stimulates tyrosine phosphorylation in T cell membrane fractions.
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| Piau et al. (1989) | interleukin 2 | | T cell | In an attempt to elucidate the biochemical pathway of signal transduction, we investigated the capacity of interleukin 2 to modulate tyrosine phosphorylation in T cell membranes. |
| Quaedackers et al. (2009) | IL-2-induced | | T cells | In contrast, IL-2-induced phosphorylated STAT5 levels were higher in bound CD4+ T cells than in non-bound CD4+ T cells. |
| Yoneda et al. (1996) | IL-2 | | T cells | On 5 min incubation of these cells with IL-2, we observed tyrosine phosphorylation of 105-kD and 110-kD proteins in NK cells and of 95-kD and 110-kD proteins in T cells. |
| Nambiar et al. (2003) | IL-2 | | T cells | We found that the overexpressed Fc epsilon RI gamma chain colocalizes with the CD3 epsilon chain on the surface membrane of T cells and that cross-linking of the new TCR/CD3 complex leads to a dramatic increase of intracytoplasmic calcium concentration, protein tyrosine phosphorylation, and IL-2 production. |
| Burns et al. (1993) | Interleukin-2 | | T lymphocytes | Interleukin-2-induced tyrosine phosphorylation of p52shc in T lymphocytes.
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| Marie et al. (2002) | IL-2 | | T lymphocytes | We found that engagement of CD46-1 or CD46-2 differentially affected CD8(+) T cell cytotoxicity, CD4(+) T cell proliferation, interleukin 2 (IL-2) and IL-10 production as well as tyrosine phosphorylation of Vav in T lymphocytes. |
| Kim et al. (2010) | IL-2 | | T-cell | To assess the relative contribution of signaling through the TCR, CD28 and these accessory molecules, we activated human T cells using soluble antibodies recognizing all four of these T-cell receptor classes (CD3, CD28, CD4/CD8, and VLA-4), and we assessed the degree of activation using higher-order flow cytometry detecting intracellular Erk1/2 phosphorylation and production of IL-2 and IFN-gamma. |
| Muńoz et al. (2008) | IL-2 | | T cells | CD38 blockade in influenza HA-specific T cells inhibited IL-2 and IFN-gamma production, PKC phosphorylation at Thr538, and PKC recruitment to the IS induced by antigen-pulsed APCs. |
| Ishii et al. (1988) | IL-2-stimulated | | T cell | The IL-2-stimulated phosphorylation was always observed in various T cell lines bearing high affinity IL-2R, but never observed in cells which express only low affinity IL-2R consisted of alpha-chain alone. |
| Kuo et al. (1992) | interleukin-2-induced | | T cells | Rapamycin completely and rapidly inhibits interleukin-2-induced phosphorylation and activation of p70 S6 kinase at concentrations comparable to those blocking S phase entry of T cells (0.05-0.2 nM). |
| Peake et al. (1999) | interleukin 2 | | T cells | The calcium flux, pattern of tyrosine phosphorylation of proteins, and interleukin 2 (IL-2) production and proliferation in response to mitogens suggested that the peripheral blood T cells activated normally. |
| Doganci et al. (2008) | IL-2 | | T cell | Although both treatments led to reduction of lung inflammation, IL-2 signaling, STAT-5 phosphorylation, and Th2-type cytokine production (IL-4 and IL-5) by lung T cells, IL-13 production and CD4(+) T cell survival were solely inhibited by the blockade of the IL-2R beta-chain. |
| Cavalcanti et al. (2010) | IL-2-induced | | T cells | When we analyzed STAT5 expression (Figure 7(a)), we found that IL-2-induced STAT5 phosphorylation was readily detectable in normal T cells (64.5 ± 5.3 /HPF and 71 ± 6.1/HPF resp.) but resulted markedly reduced in RCC patients (22.1 ± 3.3/HPF, P < .001). |
| Campbell et al. (2001) | IL-2 | | T cell | Suppression of IL-2-induced T cell proliferation and phosphorylation of STAT3 and STAT5 by tumor-derived TGF beta is reversed by IL-15.
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| Campbell et al. (2001) | IL-2 | | T cells | Using TGFbeta-producing multiple myeloma tumor cells we demonstrate that tumor-derived TGFbeta can block IL-2-induced proliferation and STAT3 and STAT5 phosphorylation in T cells. |
| Sieber et al. (2007) | IL-2 | | T cells | Similar to CsA and FK506, NCI3 inhibits dephosphorylation and nuclear translocation of NFAT, IL-2 production and proliferation of stimulated human primary T cells with IC(50) values from 2 to 4.5 microM. |
| Belkowski et al. (1998) | IL-2 | | T lymphocyte | PCNA transcription is regulated in part through tandem CRE sequences in the promoter and CRE binding proteins; IL-2 stimulates CREB phosphorylation in the resting cloned T lymphocyte, L2. |
| Joshi et al. (2006) | IL-2 mRNA | | T cells | We investigated the role of Mycobaterium leprae soluble antigen (MLSA) in the modulation of calcium signalling, phosphorylation of mitogen-activated protein (MAP) kinases and IL-2 mRNA expression in human Jurkat T cells. |
| Zhang et al. (2004) | IL-2 | | T lymphocytes | Adenosine acts through A2 receptors to inhibit IL-2-induced tyrosine phosphorylation of STAT5 in T lymphocytes: role of cyclic adenosine 3',5'-monophosphate and phosphatases.
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| Zhang et al. (2004) | IL-2 | | T cells | In this study, we show that adenosine suppressed IL-2-dependent proliferation of CTLL-2 T cells by inhibiting STAT5a/b tyrosine phosphorylation that is associated with IL-2R signaling without affecting IL-2-induced phosphorylation of Jak1 or Jak3. |
| Binné et al. (2007) | IL-2-inducible | | T cell | TIM-1 up-regulates TCR-associated signaling events, including phosphorylation of Zap70 and IL-2-inducible T cell kinase. |
| Zhao et al. (2008) | interleukin-2 | | T cells | In addition, sorafenib induced T-cell apoptosis at concentrations higher than 10 muM. sorafenib also caused G(0)/G(1) phase arrest, inhibition of CD25 and CD69 expression, interleukin-2 production and LCK phosphorylation in the T cells; all of these effects exhibited dose and time dependence. |
| Stahl et al. (2002) | IL-2 | | T cells | Furthermore, we show that IL-2 triggers a rapid, PI3K-dependent, phosphorylation of FoxO1a in primary T cells. |
| Radziewicz et al. (2010) | IL-2 | | T cells | In this study, we found that CD86 was highly expressed on HCV-specific CD8(+) T cells early in acute HCV infection and was lost on transition to chronic HCV infection; the expression of CD86 was different from other activation markers, because expression was delayed after in vitro TCR stimulation and required sufficient IL-2 signaling; and HCV-specific CD8(+) T cells in the liver of patients with chronic HCV infection were highly activated (CD69, CD38, and HLA-DR expression), but only a minority expressed CD86 or showed evidence of recent IL-2 signaling (low basal phosphorylated STAT5), despite persistent viremia. |
| Martelli et al. (2000) | interleukin-2 promoter | | T cells | As predicted, the absence of either LAT or ZAP70/Syk kinases correlated with a defect in the induction of nuclear factor of activated T cells (NFAT) transcriptional activity, activation of the interleukin-2 promoter, and ERK phosphorylation following CD2 stimulation. |
| Liang et al. (2003) | interleukin-2 | | T-cell | We show that YopH severely decreases the T-cell receptor-induced cellular tyrosine phosphorylation, ERK1/2 activity, and interleukin-2 transcriptional activity. |
| Bright et al. (1997) | IL-2 | | T lymphocytes | TGF-beta inhibits IL-2-induced tyrosine phosphorylation and activation of Jak-1 and Stat 5 in T lymphocytes.
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| Sporri et al. (2001) | IL-2-induced | | T cells | JAB/SOCS1/SSI-1 is strongly induced by IL-2 in peripheral blood T cells, and JAB/SOCS1/SSI-1 overexpression strongly inhibits IL-2-induced signal transducer and activator of transcription-5 (Stat5) phosphorylation and transcriptional activity. |
| Bianchi et al. (2000) | IL-2 | | T cells | Dexamethasone inhibited IL-2-induced DNA binding, tyrosine phosphorylation, and nuclear translocation of Stat5 in primary T cells. |
| García-Cózar et al. (1996) | IL-2 | | T cells | We show that stimulation of T cells with phytohaemagglutinin (PHA) in the presence, but not in the absence, of anti-CD28 MoAb or B7+ cells results in tyrosine phosphorylation of specific substrates, transcription of mRNA and production of IL-2 that is indistinguishable in SLE patients and healthy controls. |
| Gao et al. (2006) | interleukin-2 | | T-lymphocytes | In cultured T-lymphocytes, DBT induced markedly cell proliferation, secretion of interleukin-2 and phosphorylation of extracellular signal-regulated kinase. |
| Gelman et al. (2006) | IL-2 | | T cells | Reconstitution of MyD88-deficient primary T cells with a MyD88 transgene mutated in this motif abrogated association of PI-3 kinase with MyD88, phosphorylation of protein kinase B (Akt) and Glycogen Synthetase Kinase-3 (GSK-3), and interleukin-2 (IL-2) production. |
| Mills et al. (1993) | IL-2 | | T lymphocytes | However, we have demonstrated that the serine rich (SD) region of the cytosolic domain of IL-2R beta is also required for association of a tyrosine kinase with the IL-2R complex and that IL-2 can induce proliferation and tyrosine phosphorylation in cell lines which lack the known SRC family kinases expressed by T lymphocytes. |
| Gao et al. (2007) | interleukin-2 | | T-lymphocytes | In cultured T-lymphocytes, application of DBT markedly induced the cell proliferation, the release of interleukin-2, -6 and -10, as well as the phosphorylation of extracellular signal-regulated kinases (ERK). |
| Sanzone et al. (2003) | IL-2 | | T cells | Although phospholipase C gamma 1 phosphorylation and calcium response were both enhanced in T cells from XLP patients, phosphorylation of VAV and downstream signal transduction events such as mitogen-activated protein kinase phosphorylation and IL-2 production were diminished. |
| Lagaudričre-Gesbert et al. (1998) | IL-2 | | T cell | Addition of various co-stimuli (phorbol 12-myristate 13-acetate or monoclonal antibodies to CD3 or CD2) increases the CD82-induced morphological alterations and, reciprocally, CD82 engagement synergizes with these stimuli to induce T cell activation as indicated by both primary tyrosine phosphorylation and IL-2 production. |
| Vivier et al. (1992) | IL-2 | | T cell | Reconstituted CD16 receptor complexes triggered Ca2+ influx, tyrosine phosphorylation, and IL-2 production in stable transformants of the Jurkat T cell line. |
| Burkhardt et al. (1994) | interleukin-2 | | T cells | We found that Ig alpha and Ig beta cytoplasmic domains were able to activate Ca2+ flux, interleukin-2 secretion, and phosphorylation of the same group of cellular substrates as the TCR in transfected T cells. |
| Ishii et al. (2001) | interleukin-2 | | T cell | Our results therefore indicate a mechanism whereby CD26 engagement promotes aggregation of lipid rafts and facilitates colocalization of CD45 to T cell receptor signaling molecules p56(Lck), ZAP-70, and TCRzeta, thereby enhancing protein tyrosine phosphorylation of various signaling molecules and subsequent interleukin-2 production.
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| Musci et al. (1997) | Interleukin-2 promoter | | T cell | Previous work has demonstrated that SLP-76, a Grb2-associated tyrosine-phosphorylated protein, augments Interleukin-2 promoter activity when overexpressed in the Jurkat T cell line. |
| Sewgobind et al. (2010) | IL-2-mediated | | Treg | In this study, we examined the effect of CP-690,550 on IL-2-mediated Jak/STAT5 phosphorylation by CD4(+)CD25(bright)FoxP3(+)CD127(-/low) T cells (Treg) and CD4(+)CD25(neg) effector T cells (Teff) in kidney transplant (KTx) patients. |
| Onodera et al. (1996) | interleukin-2 | | T cell | Using a novel panel of Jurkat T cell clones that uniquely express either the smallest (CD45(0)) or the largest (CD45(ABC)) isoform, we previously demonstrated CD45 isoform-specific differences in interleukin-2 secretion and tyrosine phosphorylation of Vav. |
| Yamasaki et al. (2001) | interleukin-2 | | T cell | Overexpression of Gab2 in Jurkat cells or antigen-specific T cell hybridomas resulted in the inhibition of NF-AT activation, interleukin-2 production, and tyrosine phosphorylation. |
| Skĺlhegg et al. (1994) | IL2 mRNA | | T-cell | In the present study we have investigated the effect of cAMP on T-cell DNA synthesis, tyrosine phosphorylation of a 100 kDa protein (pp100) and IL2 mRNA expression, induced through stimulation of the TCR/CD3- and/or the CD28 molecules. |
| Skĺlhegg et al. (1994) | IL2 mRNA | | T-cell | Combined stimulation with anti-CD3 and anti-CD28, which gives a synergistic response in T-cell replication, gave pp100 phosphorylation and IL2 mRNA expression sensitive to cAMP-dependent inhibition. |
| Wong et al. (1998) | interleukin-2 gene | | T-cell | Expression of the KS chimera resulted in its autophosphorylation, the phosphorylation of cellular proteins, the upregulation of T-cell activation markers, and the induction of interleukin-2 gene synthesis in a TCR-independent fashion. |
| Yang et al. (2001) | IL-2 gene | | T cells | Using several PH domain mutants overexpressed in Jurkat T cells, we show that the Tec PH domain is required for Tec-mediated IL-2 gene induction and TCR-mediated Tec tyrosine phosphorylation. |
| Gérard et al. (2009) | IL-2 promoter | | T cell | Loss-of-function experiments using RNA interference constructs show that Dok-4 is a negative regulator of ERK phosphorylation, IL-2 promoter activity, and T cell proliferation. |
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