Gene interactions and pathways from curated databases and text-mining

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IL2 — LCK

Pathways - manually collected, often from reviews:

Text-mined interactions from Literome

Cho et al., J Biol Chem 2000 : In addition, CD38 ligation resulted in an elevated tyrosine kinase activity of the CD38 associated Lck and ultimate activation of interleukin-2 gene transcription ... Furthermore, expression of a kinase-deficient Lck mutant suppressed interleukin-2 gene activation in a dose dependent manner
Brockdorff et al., Eur Cytokine Netw 2000 (Mycosis Fungoides) : Lck is involved in interleukin-2 induced proliferation but not cell survival in human T cells through a MAP kinase independent pathway
Taichman et al., Cytokine 1992 : CTLL-2 and HT-2 LCK- and LCK ( Y505F ) -transfected cells remained dependent on IL-2 for their growth and survival in culture despite the findings that ( i ) IL-2 specifically stimulated elevations in the activity of the endogenous p56-LCK in untransfected CTLL-2 cells without affecting the activities of the other SRC-like kinases in these cells ( p59-FYN, p62-YES ) and that ( ii ) IL-2 mediated regulation of p56-LCK correlated with IL-2-driven proliferation of these T cells
Caron et al., Mol Cell Biol 1992 : Additional studies revealed that all the mutations tested, including deletion of the Src homology 3 region, abrogated the enhancement of antigen triggered interleukin-2 production by F505 p56lck , thus implying more stringent requirements for augmentation of antigen responsiveness by F505 Lck
Granelli-Piperno et al., J Autoimmun 1992 : A member of the src gene family, the lymphocyte-specific protein tyrosine kinase, p56lck , has been implicated in IL-2 production
Einspahr et al., J Leukoc Biol 1992 : The present studies indicate that IL-2 induces a rapid ( < or = 1 min ) increase in the catalytic activity of p56lck , as measured by increases in protein tyrosine kinase activity in vitro
Satoh et al., J Biol Chem 1992 : A nonreceptor-type tyrosine kinase, Lck, is associated with IL-2 receptor beta subunit, and the binding of IL-2 to its receptor induces the activation of Lck
Mills et al., Int Immunol 1992 : Activation of the IL-2R leads to serine and threonine phosphorylation of the SRC tyrosine kinase family member, LCK , and an increase in LCK tyrosine kinase activity
Torigoe et al., Proc Natl Acad Sci U S A 1992 : When combined with the recent evidence that IL-2 regulates p56lck in T cells, these results indicate that some flexibility exists in the ability of various src-like PTKs to participate in IL-2 signal transduction mechanisms and raise the possibility that lineage-specific ( T-versus B-cell ) responses to IL-2 may be determined at least in part by the repertoire of src-like PTKs expressed in the cell
Torigoe et al., Leukemia 1992 : In contrast to IL-2 's effects on p56-LCK in T-cells, studies of an IL-2-responsive cell line of the B-cell lineage that lacks p56-LCK revealed that IL-2 specifically regulates the activity of the p53/56-LYN kinase
Fukushima et al., Cell Signal 2006 : Inhibition of the Lck/Shc interaction led to the loss of IL-2 promoter activation, confirming that the role of Shc in IL-2 production requires its interaction with Lck
Torigoe et al., Blood 1992 (Leukemia, Myeloid, Acute...) : Recently, it was reported that the IL-2R ( whose p75 beta-subunit shares sequence homology with a known murine IL-3R subunit and a common beta-subunit of the human IL-3R and granulocyte-macrophage colony stimulating factor [ GM-CSF ] receptors ) can physically associate with and regulate the activity of the SRC-family PTK, p56-LCK
Yamamoto et al., Princess Takamatsu symposia 1991 : Under the same conditions, normal Lck and Lyn could not stimulate IL-2 promoter
Horak et al., Proc Natl Acad Sci U S A 1991 : The ability of IL-2 to induce p56lck activation was found to be independent of the capacity of p56lck to associate with either CD4 or CD8
Pan et al., Blood 2012 (HIV Infections) : Instead, Nef triggers Lck dependent activation of TGN associated Ras-Erk signaling to promote the production of the T lymphocyte survival factor IL-2 and to enhance virus spread
Metcalfe et al., Cell Immunol 1994 : Rapamycin did not inhibit IL2 secretion induced by TCR/CD4/p56lck , emphasizing the specific action of FK506 and cyclosporin A
Tamura et al., J Immunol 1995 : The anti-CD3 stimulation did not cause Lck activation in either the Th1 or Th2 clone, although remarkable activation was induced in both clones following anti-CD4 stimulation, indicating that Lck activation was not required for either IL-2 or IL-4 production of Th cells
Taieb et al., J Biol Chem 1993 : We show that upon mitogenic stimulation with anti-IgM antibodies and interleukin-2 , specific mRNA for p56lck becomes detectable in B cells after 24 h of activation and is followed by an increase in p56lck protein expression on days 2 and 3
Eljaafari et al., Cell Immunol 1995 : Although activation of T cells with interleukin 2 (IL-2) results in the activation of p56lck , accumulating data support the notion that Lck does not play an essential role in mitogenic signal delivery from the IL-2R ... Since this src related PTK has been shown to enhance TCR/CD3 mediated T cell responsiveness, here we investigated whether activation of Lck by IL-2 could contribute to enhance TCR/CD3 mediated T cell functions ... This increase of T cell functions was correlated with IL-2 induced p56lck activation in both dose-response and time-course experiments ... Taken together these results strongly suggest that activation of Lck by IL-2 may play a role in regulating CD3 mediated T cell functions
Vitte-Mony et al., Mol Immunol 1994 : We show here, using IL-2 dependent human natural killer cell lines, that p56lck is regulated by IL-2 in two different ways : ( 1 ) IL-2 induces a rapid increase of p56lck kinase activity as assessed in vitro ; and ( 2 ) following IL-2 stimulation, p56lck undergoes phosphorylation on serine residues that is reflected by a modification of its electrophoretic mobility in SDS-PAGE ... Furthermore, dose response experiments, and blocking studies performed with anti-IL-2R alpha antibodies, indicated that binding of IL-2 to the IL-2R beta chain was sufficient to produce these modifications of p56lck
Nishio et al., Proc Soc Exp Biol Med 1994 : The increase of coprecipitated p56lck with anti-IL-2R beta antibody by the treatment with IL-2 suggested that the affinity of p56lck to IL-2R beta was increased by IL-2 in NK-rich cells
Musso et al., J Exp Med 1994 : In fact, IFN-gamma, but not IL-2 , efficiently blocked Lsk induction by IL-4 or IL-13
Sancho et al., J Immunol 1993 : Anti-TCR/CD3 stimulation of the TCR/CD3+ J32-3.2 cells resulted in a weak stimulation of both the phosphatidyl inositol and tyrosine kinase signal transduction pathways, as measured by changes in the level of free intracellular calcium, tyrosine phosphorylation of TCR-zeta, CD3-epsilon and ZAP-70, p56lck , or p59fyn tyrosine kinase activity and IL-2 gene activation
Bröker et al., Eur J Immunol 1994 (Cell Transformation, Viral) : Since IL-2 binding to its receptor activated only the CD4 bound fraction of p56lck, the IL-2 induced p56lck activity was diminished after long-term CD4 ligation
Watts et al., J Immunol 1993 : IL-2 stimulation of T lymphocytes induces sequential activation of mitogen activated protein kinases and phosphorylation of p56lck at serine-59
Takeuchi et al., J Biol Chem 1993 : Under the same conditions, Lck did not stimulate IL-2 promoter unless it was activated by mutation ... Csk, which phosphorylates tyrosine residues in the negative regulatory sites of Src family kinases, down-regulated Fyn- and Lck mediated stimulation of the serum response element and Fyn mediated enhancement of IL-2 promoter activity
Minami et al., EMBO J 1993 : Association of p56lck with IL-2 receptor beta chain is critical for the IL-2 induced activation of p56lck ... To examine the mechanisms underlying p56lck PTK activation by IL-2 , we established a mouse pro-B cell line, BAF-B03, expressing both IL-2R beta ( either the wild-type or mutant forms ) and mouse p56lck at high levels ... Intriguingly, BAF-B03 cells expressing an IL-2R beta chain which lacks a different cytoplasmic region, the ` serine-rich ' region, also fail to activate p56lck in response to IL-2
Baldari et al., J Biol Chem 1993 : Calcium dependent cyclosporin A-sensitive activation of the interleukin-2 promoter by p56lck ... The transcription factor NF-AT mediated, at least in part, the p56lck activation of IL-2 expression
Chung et al., J Immunol 1997 : The T cell hybridoma BI-141 has been previously used to dissect the roles of Lck in Ag-induced IL-2 production ... Here we demonstrate that BI-141 undergoes apoptosis in response to TCR stimulation using Ag or anti-TCR Abs. Using a panel of BI-141 transfectants expressing constitutively activated Lck ( F505 ) or phosphotyrosine binding ( K154F505 and C156F505 ) or kinase impaired ( R273F505 ) mutants, we assess the relative requirements for Lck in TCR mediated IL-2 production and apoptosis