Interleukin 2 receptor beta chain expressed in an oligodendroglioma line binds interleukin 2 and delivers growth signal.

Okamoto, Yutaka; Minamoto, Seijiro; Shimizu, Katsuji; Mogami, Heitaro; Taniguchi, Tadatsugu

doi:10.1073/pnas.87.17.6584

Cited by 32 publications

(13 citation statements)

References 34 publications

(29 reference statements)

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“…The mouse IL-3-dependent pro-B-cell line BAF-B03 (8) and its derivatives were maintained in RPMI 1640 medium supplemented with 10% fetal calf serum and 20%o WEHI-3B conditioned medium (as a source of IL-3). BAF-B03 was stably transfected with the expression vector for the human IL-2R3, pEF/,3 (23), along with a neomycin-resistant gene by the electroporation method. After DNA transfer, neomycinresistant clones were selected as described (9).…”

Section: Methodsmentioning

confidence: 99%

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

Kono

Hatakeyama

et al. 1993

Proc. Natl. Acad. Sci. U.S.A.

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123

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The binding of interleukin 2 (IL-2) to the IL-2 receptor (IL-2R) induces a rapid increase in tyrosine phosphorylation of cellular proteins. In a previous study, we have shown that p56Ick (lck), a src-family protein tyrosine kinase (src-PTK), physically and functionally associates with the IL-2R (3 chain (IL-2Rf3). To further investigate a role of src-PTKs in IL-2 signaling, we analyzed a mouse pro-B-cell line, in which Ick is not expressed detectably. We observed that in this cell line, IL-2 induces activation of at least two src-PTKs, p59fYn (fyn) and p53/56iYn (lyn). Interestingly, stimulation of this cell line with IL-3 also induces activation of src-PTKs. The activation offtn or lyn seems to be selective for stimulation with IL-2 or IL-3 since stimulation with IL-6 fails to activate them. Furthermore, we provide evidence for the physical association offyn with IL-2R13. Taken together with previous results, our current study suggests that different src-PTKs, each of which is expressed in a cell-type-specific manner, can participate in the IL-2 signal transduction.

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Section: Methodsmentioning

confidence: 99%

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

Kono

Hatakeyama

et al. 1993

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

123

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“…IL-2R is composed of at least two subunits, the ~ (p55) and/3 (p75) chains. IL-2Rfl but not IL-2Rot has been shown to be a molecule responsible for transduction of growth signals when expressed on lymphoid and oligodendroglioma cells [2,3]. Recent studies using IL-2R~ and -/3 cDNA-transfected fibreblast cell lines have shown thai the cz and ~ subunits are not enough to forna the high affinity functional IL-2 receptor [4].…”

Section: Introduction Interleukin 2 (Il-2) Is a Well-characterized Lymentioning

confidence: 99%

IL‐2‐dependent in vivo and in vitro tyrosine phosphorylation of IL‐2 receptor γ chain

et al. 1992

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We previously reported a molecule, p64, which was tentatively named the ;, chain, copreeipitable with the fl chain of human interleukin-2 receptor (I L-2R). The present study demonstrated that the 7 chain, as ~,ell as the fl chain expressed on I L-2-responsivc cells, is phosphor'/lated on tyrosine residues in an IL-2-dependent manner in rive and in vitro. The in rive tyrosine phosphorylation of both chains was similarly induced within I mira after IL-2 stimulation, and their in vitro tyrosinc phosphorylation with the anti-lL-2Rp antibody-directed immunocomplex was also increased by treatment of cells with I L-2. These results suggest that a tyrosine kinase is associated with the/~)' subunit complex, of which activation by IL-2 may result in transduction of intracellular signals.Interleukin-2 receptor; Tyrosine kinase

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“…EcoRI-digested PCR products were cloned into the Bluescript at EcoRI site, and the sequence of the respective PCR products was confirmed. Subsequently, the cDNA fragments for DnrkS and DnrkL with EcoRI sites were ligated to the EcoRI-cleaved backbone fragment of the pEF expression vector (29), with an additional nucleotide sequence that encodes the two tandemly repeated HA epitopes, at the 5Ј end of the EcoRI-cleaved vector.…”

Section: Methodsmentioning

confidence: 99%

A Novel Drosophila Receptor Tyrosine Kinase Expressed Specifically in the Nervous System

Oishi

Sugiyama

Liu

et al. 1997

Journal of Biological Chemistry

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We report the identification and characterization of Dnrk (Drosophila neurospecific receptor kinase), a Drosophila gene encoding a putative receptor tyrosine kinase (RTK) highly related to the Trk and Ror families of RTKs. During Drosophila embryogenesis, the Dnrk gene is expressed specifically in the developing nervous system. The Dnrk protein possesses two conserved cysteine-containing domains and a kringle domain within its extracellular domain, resembling those observed in Ror family RTKs (Ror1, Ror2, and a Drosophila Ror, Dror). This protein contains the catalytic tyrosine kinase (TK) domain with two putative ATP-binding motifs, resembling those observed in another Drosophila RTK (Dtrk) that mediates homophilic cell adhesion. The TK domain of Dnrk, expressed in bacteria or mammalian cells, exhibits apparent autophosphorylation activities in vitro. The TK domain lacking the distal ATP-binding motif also exhibits autophosphorylation activity, yet to a lesser extent. In addition to its TK activity, there are several putative tyrosine-containing motifs that upon phosphorylation may interact with Src homology 2 regions of other signaling molecules. Collectively, these results suggest that Dnrk may play an important role in neural development during Drosophila embryogenesis.

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Interleukin 2 receptor beta chain expressed in an oligodendroglioma line binds interleukin 2 and delivers growth signal.

Cited by 32 publications

References 34 publications

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.

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.

IL‐2‐dependent in vivo and in vitro tyrosine phosphorylation of IL‐2 receptor γ chain

A Novel Drosophila Receptor Tyrosine Kinase Expressed Specifically in the Nervous System

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