Functional coupling of the src-family protein tyrosine kinases p59fyn and p53/56lyn with the interleukin 2 receptor: implications for redundancy and pleiotropism in cytokine signal transduction.

Kobayashi, Naoki; Kono, Toru; Hatakeyama, Masanori; Minami, Yasuhiro; Miyazaki, Tatsuya; Perlmutter, Roger M.; Taniguchi, Tadatsugu

doi:10.1073/pnas.90.9.4201

Cited by 123 publications

(42 citation statements)

References 47 publications

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“…Fyn Ϫ/Ϫ mice have normal T cell development but two recent studies have found that the number of NKT cells is reduced in these mice (42,43). It has been demonstrated that Fyn binds to CD3, and Lck to CD4 and CD8␣; however, both Lck and Fyn can bind the IL-2R␤ (44,45). LAK cells generated from Fyn Ϫ/Ϫ mice had equivalent numbers of NK1.1 ϩ CD8 ϩ T cells to those derived from B6 mice.…”

Section: Cd8mentioning

confidence: 99%

CD8+ T Cells Rapidly Acquire NK1.1 and NK Cell-Associated Molecules Upon Stimulation In Vitro and In Vivo

Assarsson

Kambayashi

Sandberg

et al. 2000

The Journal of Immunology

131

108

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NKT cells express both NK cell-associated markers and TCR. Classically, these NK1.1+TCRαβ+ cells have been described as being either CD4+CD8− or CD4−CD8−. Most NKT cells interact with the nonclassical MHC class I molecule CD1 through a largely invariant Vα14-Jα281 TCR chain in conjunction with either a Vβ2, -7, or -8 TCR chain. In the present study, we describe the presence of significant numbers of NK1.1+TCRαβ+ cells within lymphokine-activated killer cell cultures from wild-type C57BL/6, CD1d1−/−, and Jα281−/− mice that lack classical NKT cells. Unlike classical NKT cells, 50–60% of these NK1.1+TCRαβ+ cells express CD8 and have a diverse TCR Vβ repertoire. Purified NK1.1−CD8α+ T cells from the spleens of B6 mice, upon stimulation with IL-2, IL-4, or IL-15 in vitro, rapidly acquire surface expression of NK1.1. Many NK1.1+CD8+ T cells had also acquired expression of Ly-49 receptors and other NK cell-associated molecules. The acquisition of NK1.1 expression on CD8+ T cells was a particular property of the IL-2Rβ+ subpopulation of the CD8+ T cells. Efficient NK1.1 expression on CD8+ T cells required Lck but not Fyn. The induction of NK1.1 on CD8+ T cells was not just an in vitro phenomenon as we observed a 5-fold increase of NK1.1+CD8+ T cells in the lungs of influenza virus-infected mice. These data suggest that CD8+ T cells can acquire NK1.1 and other NK cell-associated molecules upon appropriate stimulation in vitro and in vivo.

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Section: Cd8mentioning

confidence: 99%

CD8+ T Cells Rapidly Acquire NK1.1 and NK Cell-Associated Molecules Upon Stimulation In Vitro and In Vivo

Assarsson

Kambayashi

Sandberg

et al. 2000

The Journal of Immunology

131

108

View full text Add to dashboard Cite

show abstract

“…The Src kinase family members Lck and Fyn associate with the IL-2R β chain (28,29), and become phosphorylated upon activation of the receptor (30). Phosphorylation of these kinases can lead to the recruitment of other proteins involved in signaling, including PI 3-kinase (31,32).…”

Section: Dq 65-79 Does Not Inhibit Expression or Phosphorylation Of Tmentioning

confidence: 99%

A human class II MHC–derived peptide antagonizes phosphatidylinositol 3-kinase to block IL-2 signaling

Boytim¹,

Lilly²,

Drouvalakis³

et al. 2000

J. Clin. Invest.

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“…Among Src-family PTKs, Fyn and Lyn are major PTKs expressed in F7 cells (Torigoe et al, 1992b), and IL-2 induces activation of both Src-PTKs (Kobayashi et al, 1993). To assess the possibility of tyrosine phosphorylation of SHP-2 by the Src family PTKs, co-transfection experiments of SHP-2 with the respective Src-family PTKs in COS cells were performed.…”

Section: Shp-2 Is Preferentially Tyrosine Phosphorylated By Lyn In Comentioning

confidence: 99%

Interleukin-2 induces tyrosine phosphorylation of SHP-2 through IL-2 receptor β chain

et al. 1997

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Coupling of interleukin-2 (IL-2) to the IL-2 receptor (IL-2R) induces rapid increase in tyrosine phosphorylation of cellular substrates through activation of non-receptor protein tyrosine kinases. Here, we report that stimulation through the IL-2R induced tyrosine phosphorylation of the SH2-containing protein-tyrosine phosphatase SHP-2 in F7, a hematopoietic BAF-B03 transfectant clone expressing the IL-2Rb chain. The tyrosine phosphorylation of SHP-2 was speci®c since another protein-tyrosine phosphatase SHP-1, which is structurally homologous to SHP-2, was not tyrosine phosphorylated. The IL-2-induced tyrosine phosphorylation of SHP-2 required the acidic region within the IL-2Rb chain where Src-family PTKs interact. Though the serine-rich region within IL2Rb chain was also required for the phosphorylation of SHP-2, Jak3 activation was dispensable. In COS-7 cells, co-expression of SHP-2 with Lyn resulted in increased tyrosine phosphorylation levels of SHP-2, whereas coexpression of SHP-2 with Fyn failed to alter the levels signi®cantly. Considering that Lyn and Fyn are major Src-family PTKs expressed in BAF-B03 cells, our data suggest that Lyn may be principally responsible for the tyrosine phosphorylation of SHP-2 in F7 cells. Furthermore, the IL-2 stimulation also induced tyrosine phosphorylation of SHP-2 in the human IL-2-dependent T-cell line ILT-Mat. Taken together, these studies demonstrate an involvement of SHP-2 in the IL-2-mediated signaling events through the activation of speci®c PTKs.

show abstract

Functional coupling of the src-family protein tyrosine kinases p59fyn and p53/56lyn with the interleukin 2 receptor: implications for redundancy and pleiotropism in cytokine signal transduction.

Cited by 123 publications

References 47 publications

CD8+ T Cells Rapidly Acquire NK1.1 and NK Cell-Associated Molecules Upon Stimulation In Vitro and In Vivo

CD8+ T Cells Rapidly Acquire NK1.1 and NK Cell-Associated Molecules Upon Stimulation In Vitro and In Vivo

A human class II MHC–derived peptide antagonizes phosphatidylinositol 3-kinase to block IL-2 signaling

Interleukin-2 induces tyrosine phosphorylation of SHP-2 through IL-2 receptor β chain

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