Viewing negative mentions of phosphorylation in T cells

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Isakov et al. (1996)ZAP-70T cellIn contrast to the T cell protein tyrosine kinase, Lck, ZAP-70 did not phosphorylate the cytoplasmic portion of the TCRzeta chain or short peptides corresponding to the CD3epsilon or the TCRzeta immunoreceptor tyrosine-based activation motifs.
Tsukamoto et al. (2006)LATT cellUsing this system, we demonstrated that the T cell clone stimulated with APL/HLA-DR4 complexes presented at an excessive density provoked the up-regulation of CD69, IL-2 production and proliferation, but no detectable phosphorylation of ZAP-70/LAT/SLP-76.
Fagerholm et al. (2002)PKCT cellsSer-756, a residue not phosphorylated by PKC isoforms, also became phosphorylated in T cells after phorbol ester stimulation.
McKay et al. (1999)LATT cellsThe targets for the unresponsive state appear to be diminished Lck activation and absent ZAP-70 and LAT (linker for activation of T cells) phosphorylation.
Ng et al. (1997)lckT-cellsThus CD45 is intrinsically a much more active phosphatase than RPTPalpha, which provides one reason why RPTPalpha cannot effectively dephosphorylate p56(lck) and substitute for CD45 in T-cells.
Oetken et al. (1994)p56lckT cellRecently, we found that p50csk specifically phosphorylates the negative regulatory Tyr-505 of the T cell-specific src-family kinase p56lck, and thereby suppresses its catalytic activity.
Miah et al. (2004)NFATT cellsAntigen-induced phosphorylation of Vav1, activation of Rac1, extracellular signal regulated kinase (ERK), c-Jun N-terminal kinase (JNK), p38 mitogen activated protein kinase (MAPK), inhibitor of nuclear factor kappaB kinase (IKK) and nuclear factor of activated T cells (NFAT) were all impaired in the cells over-expressing the cherubism mutants of 3BP2.
Nika et al. (2004)MAPT-cellsThe HePTP (haematopoietic protein tyrosine phosphatase) is a negative regulator of the ERK2 (extracellular signal-regulated protein kinase 2) and p38 MAP kinases (mitogen-activated protein kinases) in T-cells.
Han et al. (2003)Y334FT cellsZAP-70 phosphorylated HIP-55 at Tyr-334 and Tyr-344 in vitro and in vivo, and the HIP-55 mutant (Y334F/Y344F) was not tyrosine-phosphorylated in stimulated T cells.
Némorin et al. (2001)dokT cellsIn T cells, the two members that are predominantly expressed, p56(dok) and p62(dok), are tyrosine phosphorylated upon CD2 or CD28 stimulation, but not upon CD3 ligation.
Wiese et al. (1996)SrcT cellA dramatic increase of Lck activity was also observed in T cell lines transfected with Tip. p60fyn and p53/56lyn, the other Src-related kinases expressed in H. saimiri transformed T cells, did not phosphorylate Tip, and they were not activated by the protein.
Waldman et al. (1992)HLA class II antigenT cellFurthermore, we demonstrate the heretofore undescribed phenomenon of CD4+ T cell activation in the absence of serologically detectable HLA class II antigen.
Fujimaki et al. (2001)CD4T-cellAfter restimulation, it was markedly dephosphorylated in APB CD4+ T-cell blasts but not in thymic CD4+ T-cell blasts.
Leemput et al. (2009)ATMT cellsIn A-T cells, shared ATM and ATR substrates are not phosphorylated efficiently in response to IR because ATM is absent, causing a delay in end resection.
Höllsberg et al. (1994)pRbT cellHere we report that HTLV-I-infected but not uninfected T cell clones have hyperphosphorylated pRb consistent with viral-induced T cell activation.
Badour et al. (2004)WASpT cellsTCR-induced WASp tyrosine phosphorylation was also disrupted in T cells lacking Fyn, a kinase shown here to bind, colocalize with, and phosphorylate WASp.
McKay et al. (1999)ZAP-70T cellsThe targets for the unresponsive state appear to be diminished Lck activation and absent ZAP-70 and LAT (linker for activation of T cells) phosphorylation.
Judd et al. (2002)LATLATAdditionally, unlike SLP-76, LAT is not tyrosine phosphorylated after fibrinogen binding to integrin alphaIIbbeta3, and collagen-stimulated platelets deficient in LAT spread normally on fibrinogen-coated surfaces.
Wiese et al. (1996)TipT cellA dramatic increase of Lck activity was also observed in T cell lines transfected with Tip. p60fyn and p53/56lyn, the other Src-related kinases expressed in H. saimiri transformed T cells, did not phosphorylate Tip, and they were not activated by the protein.
Yi et al. (2000)CblT cellsWhen exposed to the anergy protocol, lupus T cells, in marked contrast to normal T cells, did not phosphorylate Cbl/Cbl-b but continued to express strongly phosphorylated extracellular signal-regulated kinase (ERK); U0126, a specific inhibitor of mitogen-activated protein kinase kinase --> ERK, could block both the early and the prolonged hyperexpression of CD40L.
Oetken et al. (1994)p50cskT cellRecently, we found that p50csk specifically phosphorylates the negative regulatory Tyr-505 of the T cell-specific src-family kinase p56lck, and thereby suppresses its catalytic activity.
Lassen et al. (2006)RNA pol II complexesT cellsThe nuclear retention of MS HIV-1 RNAs in resting CD4+ T cells may result from inefficient transcription by RNA pol II complexes that are not properly phosphorylated on the C-terminal domain due to the absence of Tat and associated host factors.
Tsukamoto et al. (2006)SLP-76T cellUsing this system, we demonstrated that the T cell clone stimulated with APL/HLA-DR4 complexes presented at an excessive density provoked the up-regulation of CD69, IL-2 production and proliferation, but no detectable phosphorylation of ZAP-70/LAT/SLP-76.
Pitcher et al. (2003)zetaT cellThese results suggest that the mechanism of T cell antagonism is independent of the two phosphorylated TCR zeta derivatives.
Graeler et al. (2003)c-FosT cellThe same PKCepsilon inhibitors blocked S1P-evoked increases in T cell nuclear levels of c-Fos and phosphorylated c-Jun and JunD after 24 h, but not 1 h.
Bottini et al. (2002)LMPTPT cellOur results indicate that LMPTP, like CD45, dephosphorylates a negative regulatory tyrosine site in a protein-tyrosine kinase and thereby strengthens T cell receptor signaling.
Autero et al. (1994)cellT-cellThis residue was not phosphorylated by T-cell PTKs p56lck and p59fyn.
Tagawa et al. (1991)protein kinase C activatorT cellMurine T cell surface antigens, CD4 and CD8 are phosphorylated in response to phorbol 12-myristate 13-acetate, a protein kinase C activator, but not phosphorylated after concanavalin A, Ca2+ ionophore or dibutyryl-cAMP treatment.
Cohen et al. (1983)arabinosylGTPT cellsDeoxyguanosine and arabinosylguanine are phosphorylated to deoxyGTP and arabinosylGTP, respectively, by T cells but not by other cell types.
Marie-Cardine et al. (1995)alpha-tubulinT lymphocytesBy contrast, in untransformed resting human T lymphocytes alpha-tubulin is not detectable as a tyrosine phosphorylated protein.
Leemput et al. (2009)ATRT cellsIn A-T cells, shared ATM and ATR substrates are not phosphorylated efficiently in response to IR because ATM is absent, causing a delay in end resection.
Tsukamoto et al. (2006)ZAP-70T cellUsing this system, we demonstrated that the T cell clone stimulated with APL/HLA-DR4 complexes presented at an excessive density provoked the up-regulation of CD69, IL-2 production and proliferation, but no detectable phosphorylation of ZAP-70/LAT/SLP-76.
Isakov et al. (1996)LckT cellIn contrast to the T cell protein tyrosine kinase, Lck, ZAP-70 did not phosphorylate the cytoplasmic portion of the TCRzeta chain or short peptides corresponding to the CD3epsilon or the TCRzeta immunoreceptor tyrosine-based activation motifs.
Graeler et al. (2003)JunDT cellThe same PKCepsilon inhibitors blocked S1P-evoked increases in T cell nuclear levels of c-Fos and phosphorylated c-Jun and JunD after 24 h, but not 1 h.
Dong et al. (2010)Lck Tyr505T cellsAs in primary T cells, in Hut-78 cells, Lck Tyr505 was basally phosphorylated and not dephosphorylated upon TCR stimulation.
Wu et al. (2008)cofilinT cellsIn unstimulated resting CD4 T cells, cofilin exists largely as a phosphorylated inactive form.
Hehner et al. (2000)MLK3T-cellAccordingly, endogenous MLK3 was phosphorylated and activated by T-cell costimulation but not by treatment of cells with tumor necrosis factor alpha or interleukin-1.
Graeler et al. (2003)c-JunT cellThe same PKCepsilon inhibitors blocked S1P-evoked increases in T cell nuclear levels of c-Fos and phosphorylated c-Jun and JunD after 24 h, but not 1 h.
Muthusamy and Leiden (1998)CREBT cellsT cells lacking the p56(lck) tyrosine kinase failed to phosphorylate CREB in response to TCR engagement.
Pitcher et al. (2003)TCRT cellThese results suggest that the mechanism of T cell antagonism is independent of the two phosphorylated TCR zeta derivatives.
Altan-Bonnet et al. (2005)ppERKT cellsControl experiments confirmed that the intracellular staining protocol we used was capable of detecting doubly phosphorylated, kinase-active ERK (ppERK) levels within T cells that were lower or higher than the fixed level seen among the responding cells in Figure 1A (Figure S2), indicating that the quantitatively constant nature of this signaling response is an inherent property of the T cells and not an artifact of the measurement technique.
Han et al. (2003)Y344FT cellsZAP-70 phosphorylated HIP-55 at Tyr-334 and Tyr-344 in vitro and in vivo, and the HIP-55 mutant (Y334F/Y344F) was not tyrosine-phosphorylated in stimulated T cells.
Han et al. (2003)HIP-55T cellsZAP-70 phosphorylated HIP-55 at Tyr-334 and Tyr-344 in vitro and in vivo, and the HIP-55 mutant (Y334F/Y344F) was not tyrosine-phosphorylated in stimulated T cells.
Ng et al. (1997)RPTPalphaT-cellsThus CD45 is intrinsically a much more active phosphatase than RPTPalpha, which provides one reason why RPTPalpha cannot effectively dephosphorylate p56(lck) and substitute for CD45 in T-cells.
Ling et al. (1998)IkappaBalphaT cellsMoreover, the phosphorylated form of IkappaBalpha detected in normal T cells after activation is absent in patient T cells.
Wu et al. (2008)cofilinT cellsIn unstimulated resting CD4 T cells, cofilin exists largely as a phosphorylated inactive form.
Eriksen et al. (2001)STAT3T cellsWe show that (1) STAT3 (a transcription factor known to regulate IL-2Ralpha transcription) is constitutively tyrosine-phosphorylated in SS tumor cells, but not in non-malignant T cells; (2) STAT3 binds constitutively to a STAT-binding sequence in the promotor of the IL-2Ralpha gene; (3) the Janus kinase inhibitor, tyrphostine AG490, inhibits STAT3 activation, STAT3 DNA binding, and IL-2Ralpha mRNA and protein expression in parallel; and (4) tyrphostine AG490 inhibits IL-2 driven mitogenesis and triggers apoptosis in SS tumor cells.
Cho et al. (2004)ZAP70T cellsTCR zeta chains in Tip-expressing T cells were initially phosphorylated to recruit ZAP70 molecule upon TCR stimulation, but the recruited ZAP70 kinase was not subsequently phosphorylated, resulting in TCR complexes that were stably associated with inactive ZAP70 kinase.
Némorin et al. (2001)p62T cellsIn T cells, the two members that are predominantly expressed, p56(dok) and p62(dok), are tyrosine phosphorylated upon CD2 or CD28 stimulation, but not upon CD3 ligation.
Difilippantonio et al. (2007)S343T cellWe find that T cell and oocyte development, as well as DNA damage-induced G2/M and S phase checkpoint arrest and radiation survival are dependent on the N-terminal forkhead-associated domain, but not on the principal residues phosphorylated by ATM (S278 and S343) or on the evolutionarily conserved C-terminal region of Nbs1.
Difilippantonio et al. (2007)S278T cellWe find that T cell and oocyte development, as well as DNA damage-induced G2/M and S phase checkpoint arrest and radiation survival are dependent on the N-terminal forkhead-associated domain, but not on the principal residues phosphorylated by ATM (S278 and S343) or on the evolutionarily conserved C-terminal region of Nbs1.
Difilippantonio et al. (2007)ATMT cellWe find that T cell and oocyte development, as well as DNA damage-induced G2/M and S phase checkpoint arrest and radiation survival are dependent on the N-terminal forkhead-associated domain, but not on the principal residues phosphorylated by ATM (S278 and S343) or on the evolutionarily conserved C-terminal region of Nbs1.
Farber et al. (1997)ZAP-70T cellsFollowing stimulation through TCR/CD3, memory CD4 T cells produce fewer species of tyrosine-phosphorylated substrates and fail to phosphorylate ZAP-70, yet unphosphorylated ZAP-70 can associate with the TCR/CD3 complex.
Duhant et al. (2005)ERK1T cellsIn primary human CD4+ T cells, as shown in Figures 3A and B, a rapid phosphorylation of ERK2 (p42), p38 and PKB occurred following stimulation by anti-CD3/CD28 antibodies, while no phosphorylation of ERK1 could be detected.
Ng et al. (1997)CD45T-cellsThus CD45 is intrinsically a much more active phosphatase than RPTPalpha, which provides one reason why RPTPalpha cannot effectively dephosphorylate p56(lck) and substitute for CD45 in T-cells.
Geahlen and Harrison (1984)112 kDa proteinT cellsThe phosphorylation of 112 kDa protein is greatly reduced or absent in unstimulated T cells.
Jackman et al. (2009)STAT-3T cellsThe observed loss of immunogenicity was nearly complete, with UV-irradiated cells stimulating barely measurable interferon-gamma production and no detectable STAT-3, STAT-5, or CD3-epsilon phosphorylation in allospecific primed T cells.
Dong et al. (2010)TCRT cellsAs in primary T cells, in Hut-78 cells, Lck Tyr505 was basally phosphorylated and not dephosphorylated upon TCR stimulation.
Miah et al. (2004)activated protein kinaseT cellsAntigen-induced phosphorylation of Vav1, activation of Rac1, extracellular signal regulated kinase (ERK), c-Jun N-terminal kinase (JNK), p38 mitogen activated protein kinase (MAPK), inhibitor of nuclear factor kappaB kinase (IKK) and nuclear factor of activated T cells (NFAT) were all impaired in the cells over-expressing the cherubism mutants of 3BP2.
Jaso-Friedmann et al. (1995)p56lckT-cellUnlike their mammalian T-cell and natural killer (NK) cell counterparts, NCC p56lck did not autophosphorylate on tyrosine residues.
Hindley and Kolch (2007)BADT-cellsWhile neither Raf-1 nor B-Raf could phosphorylate BAD, they enhanced the ability of PKCtheta to interact with BAD and to phosphorylate BAD in vitro and in vivo, suggesting a new role for Raf proteins in T-cells by targeting PKCtheta to interact with and phosphorylate BAD.
Omura-Minamisawa et al. (2000)pRbT-cellPreviously, we reported that most primary T-cell acute lymphoblastic leukemia (T-ALL) harbored p16 inactivation and hyperphosphorylated pRb without cyclin Ds or CDK4/6 alterations.
Jackman et al. (2009)STAT-5T cellsThe observed loss of immunogenicity was nearly complete, with UV-irradiated cells stimulating barely measurable interferon-gamma production and no detectable STAT-3, STAT-5, or CD3-epsilon phosphorylation in allospecific primed T cells.
Hindley and Kolch (2007)Raf-1T-cellsWhile neither Raf-1 nor B-Raf could phosphorylate BAD, they enhanced the ability of PKCtheta to interact with BAD and to phosphorylate BAD in vitro and in vivo, suggesting a new role for Raf proteins in T-cells by targeting PKCtheta to interact with and phosphorylate BAD.
Galley et al. (1997)TCRzetaT cellThe TCRzeta or CD3epsilon chains were found not to be phosphorylated and T. parva-transformed T cells were resistant to inhibitors that block the early steps of T cell activation.
Bright et al. (1997)IL-2T cellsWe show here that treatment of activated T cells with TGF-beta inhibited IL-2-induced tyrosine phosphorylation and activation of Jak-1 and Stat 5 but not Jak-3 and Stat 3.
Autero et al. (1994)p56lckT-cellThis residue was not phosphorylated by T-cell PTKs p56lck and p59fyn.
Madrenas et al. (1997)ZAP-70T cellsIn addition, T cells exposed to wild-type ligand in the presence of anti-CD4 antibodies show a pattern of TCR signaling resembling that seen using partial agonists, with predominant accumulation of the p21 tyrosine-phosphorylated form of TCR-zeta, reduced tyrosine phosphorylation of CD3epsilon, and no detectable phosphorylation of ZAP-70.
Bright et al. (1997)Jak-1T cellsWe show here that treatment of activated T cells with TGF-beta inhibited IL-2-induced tyrosine phosphorylation and activation of Jak-1 and Stat 5 but not Jak-3 and Stat 3.
Bottini et al. (2002)CD45T cellOur results indicate that LMPTP, like CD45, dephosphorylates a negative regulatory tyrosine site in a protein-tyrosine kinase and thereby strengthens T cell receptor signaling.
Jackman et al. (2009)interferon-gammaT cellsThe observed loss of immunogenicity was nearly complete, with UV-irradiated cells stimulating barely measurable interferon-gamma production and no detectable STAT-3, STAT-5, or CD3-epsilon phosphorylation in allospecific primed T cells.
Bright et al. (1997)Stat 3T cellsWe show here that treatment of activated T cells with TGF-beta inhibited IL-2-induced tyrosine phosphorylation and activation of Jak-1 and Stat 5 but not Jak-3 and Stat 3.
Hindley and Kolch (2007)B-RafT-cellsWhile neither Raf-1 nor B-Raf could phosphorylate BAD, they enhanced the ability of PKCtheta to interact with BAD and to phosphorylate BAD in vitro and in vivo, suggesting a new role for Raf proteins in T-cells by targeting PKCtheta to interact with and phosphorylate BAD.
Nika et al. (2004)p38T-cellsThe HePTP (haematopoietic protein tyrosine phosphatase) is a negative regulator of the ERK2 (extracellular signal-regulated protein kinase 2) and p38 MAP kinases (mitogen-activated protein kinases) in T-cells.
Isakov et al. (1996)TCRzeta chainT cellIn contrast to the T cell protein tyrosine kinase, Lck, ZAP-70 did not phosphorylate the cytoplasmic portion of the TCRzeta chain or short peptides corresponding to the CD3epsilon or the TCRzeta immunoreceptor tyrosine-based activation motifs.
Jackman et al. (2009)CD3-epsilonT cellsThe observed loss of immunogenicity was nearly complete, with UV-irradiated cells stimulating barely measurable interferon-gamma production and no detectable STAT-3, STAT-5, or CD3-epsilon phosphorylation in allospecific primed T cells.
Bukrinsky (2008)cofilinT cellsYoder et al. reported that in resting T cells, cofilin was largely phosphorylated (inactive), but was activated by dephosphorylation within minutes after HIV infection [11].
Bright et al. (1997)Jak-3T cellsWe show here that treatment of activated T cells with TGF-beta inhibited IL-2-induced tyrosine phosphorylation and activation of Jak-1 and Stat 5 but not Jak-3 and Stat 3.
Bright et al. (1997)Stat 5T cellsWe show here that treatment of activated T cells with TGF-beta inhibited IL-2-induced tyrosine phosphorylation and activation of Jak-1 and Stat 5 but not Jak-3 and Stat 3.
Miah et al. (2004)MAPKT cellsAntigen-induced phosphorylation of Vav1, activation of Rac1, extracellular signal regulated kinase (ERK), c-Jun N-terminal kinase (JNK), p38 mitogen activated protein kinase (MAPK), inhibitor of nuclear factor kappaB kinase (IKK) and nuclear factor of activated T cells (NFAT) were all impaired in the cells over-expressing the cherubism mutants of 3BP2.
Némorin et al. (2001)p56T cellsIn T cells, the two members that are predominantly expressed, p56(dok) and p62(dok), are tyrosine phosphorylated upon CD2 or CD28 stimulation, but not upon CD3 ligation.
Autero et al. (1994)p59fynT-cellThis residue was not phosphorylated by T-cell PTKs p56lck and p59fyn.
Jaso-Friedmann et al. (1995)NCCT-cellUnlike their mammalian T-cell and natural killer (NK) cell counterparts, NCC p56lck did not autophosphorylate on tyrosine residues.
Oetken et al. (1994)src-family kinaseT cellRecently, we found that p50csk specifically phosphorylates the negative regulatory Tyr-505 of the T cell-specific src-family kinase p56lck, and thereby suppresses its catalytic activity.
Bottini et al. (2002)kinaseT cellOur results indicate that LMPTP, like CD45, dephosphorylates a negative regulatory tyrosine site in a protein-tyrosine kinase and thereby strengthens T cell receptor signaling.
Bottini et al. (2002)cell receptorT cellOur results indicate that LMPTP, like CD45, dephosphorylates a negative regulatory tyrosine site in a protein-tyrosine kinase and thereby strengthens T cell receptor signaling.
Nika et al. (2004)kinase 2T-cellsThe HePTP (haematopoietic protein tyrosine phosphatase) is a negative regulator of the ERK2 (extracellular signal-regulated protein kinase 2) and p38 MAP kinases (mitogen-activated protein kinases) in T-cells.
Nika et al. (2004)kinasesT-cellsThe HePTP (haematopoietic protein tyrosine phosphatase) is a negative regulator of the ERK2 (extracellular signal-regulated protein kinase 2) and p38 MAP kinases (mitogen-activated protein kinases) in T-cells.
Eriksen et al. (2001)factorT cellsWe show that (1) STAT3 (a transcription factor known to regulate IL-2Ralpha transcription) is constitutively tyrosine-phosphorylated in SS tumor cells, but not in non-malignant T cells; (2) STAT3 binds constitutively to a STAT-binding sequence in the promotor of the IL-2Ralpha gene; (3) the Janus kinase inhibitor, tyrphostine AG490, inhibits STAT3 activation, STAT3 DNA binding, and IL-2Ralpha mRNA and protein expression in parallel; and (4) tyrphostine AG490 inhibits IL-2 driven mitogenesis and triggers apoptosis in SS tumor cells.
Fagerholm et al. (2002)isoformsT cellsSer-756, a residue not phosphorylated by PKC isoforms, also became phosphorylated in T cells after phorbol ester stimulation.