Interleukin 3 and phorbol ester stimulate tyrosine phosphorylation of overlapping substrate proteins

Ferris, Douglas K.; Willette-Brown, Jami; Martensen, Todd M.; Farrar, William L.

doi:10.1016/0014-5793(89)80273-x

Cited by 13 publications

(6 citation statements)

References 35 publications

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“…IL 3-induced phosphorylation of a 140 kDa protein in a murine cell line was originally reported by Koyasu et al (1987) and has been confirmed by the findings of several groups (Morla et al, 1988;Isfort et al, 1988;Sorenson et al, 1989a,b;Schreurs et al, 1989;Ferris et al, 1989). Two recent reports indicate that the 140 kDa tyrosyl-phosphoprotein observed after IL 3 stimulation may be the IL 3 receptor (Sorenson et al, 1989b;Isfort et al, 1988 (Fig.…”

Section: Discussionsupporting

confidence: 63%

“…Previouswork addressing signal transduction byhaematopoietic cytokines has focused primarily on colony-stimulating-factorinduced phosphorylation in mouse myeloid cell lines (Evans et al, 1987;Sorenson et al, 1989a;Ferris et al, 1988Ferris et al, , 1989. Though mouse cell lines have served as a useful tool in elucidating the biology of the haematopoietic cytokines, ultimately it is critical to develop human models with which to conduct such studies.…”

Section: Introductionmentioning

confidence: 99%

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Signal transduction of human interleukin 3 and granulocyte-macrophage colony-stimulating factor through serine and tyrosine phosphorylation

Linnekin

Farrar

1990

Biochemical Journal

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To elucidate the rapid events in signal transduction of human granulocyte-macrophage colony-stimulating factor (GM-CSF) and interleukin 3 (IL 3), we examined phosphorylation of proteins on both serine and tyrosine residues in a cytokine-stimulated human myeloid cell line. We found increases in tyrosine phosphorylation within 30 s of stimulation with GM-CSF or IL 3, with peak responses occurring within 2 min. IL 3 and GM-CSF also induced serine phosphorylation, though 10 min of stimulation was required for maximum phosphate incorporation. Interestingly, both IL 3 and GM-CSF stimulated phosphate incorporation in identical substrates, a 68 kDa seryl-phosphoprotein (p68) and a 140 kDa tyrosyl-phosphoprotein (pl40). Treatment of AML 193 cells with phorbol myristate acetate resulted in serine phosphorylation of p68; however, p140 was not phosphorylated on tyrosine. Depletion of protein kinase C isoenzymes with high concentrations of phorbol myristate acetate resulted in p68 phosphorylation, which was not further increased by IL 3 or GM-CSF. In contrast, cytokine-induced phosphorylation on tyrosine of p140 was observed after protein kinase C depletion. These data demonstrate the co-ordinate yet independent serine and tyrosine phosphorylation in IL 3-and GM-CSF-treated human myeloid cells, and thus suggest a common set of protein kinases stimulated by each separate ligand.

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Section: Discussionsupporting

confidence: 63%

Section: Introductionmentioning

confidence: 99%

Signal transduction of human interleukin 3 and granulocyte-macrophage colony-stimulating factor through serine and tyrosine phosphorylation

Linnekin

Farrar

1990

Biochemical Journal

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“…Disparate findings have been reported regarding the signaling pathways involved in this atypical tyrosine phosphorylation. Several studies using phorbol esters (22,23,64) have indicated a possible role for PKC in tyrosine phosphorylation. In permeabilized neutrophils, GTP-yS-stimulated increase in P-Tyr-protein levels was not mimicked by exogenous diacylglycerols (51), but the role of Ca2+ was not examined.…”

Section: Discussionmentioning

confidence: 99%

Angiotensin II stimulates protein-tyrosine phosphorylation in a calcium-dependent manner.

Huckle¹,

Prokop²,

Dy³

et al. 1990

Mol. Cell. Biol.

121

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Cellular responses to epidermal growth factor (EGF) are dependent on the tyrosine-specific protein kinase activity of the cell-surface EGF receptor. Previous studies using WB rat liver epithelial cells have detected at least 10 proteins whose phosphotyrosine (P-Tyr) content is increased by EGF. In this study, we have examined alternate modes of activating tyrosine phosphorylation. Treatment of WB cells with hormones linked to Ca2+ mobilization and protein kinase C (PKC) activation, including angiotensin II, [Arg8]vasopressin, or epinephrine, stimulated rapid (<15-s) and transient increases in the P-Tyr content of several proteins (p120/125, p75/78, and p66). These proteins, detected by anti-P-Tyr immunoblotting, were similar in molecular weight to a subset of EGF-sensitive P-Tyr-containing proteins (P-Tyr-proteins all P-Tyr-proteins in response to angiotensin II, thapsigargin, or ionophores, as well as two EGF-stimulated P-Tyr-proteins. The majority of EGF-stimulated P-Tyr-proteins were not affected by BAPTA. These studies indicate that angiotensin II can alter protein-tyrosine phosphorylation in a manner that is secondary to, and apparently dependent on, Ca2+ mobilization. Thus, ligands such as EGF and angiotensin II, which act through distinct types of receptors, may activate secondary pathways involving tyrosine phosphorylation. These results also raise the possibility that certain growth-promoting effects of Ca2+-mobilizing agents such as angiotensin H may be mediated via tyrosine phosphorylation.Reversible phosphorylation of proteins is a major mechanism by which metabolic processes are regulated. Phosphorylation on serine and threonine residues, which together account for >99% of total cellular protein phosphate, are recognized as key elements in the regulation of such diverse pathways as glycogen metabolism, protein biosynthesis, and cell surface receptor signaling (19). Phosphorylation on tyrosine residues, which accounts for <0.5% of proteinbound phosphate (12), has been linked broadly with the control of cell proliferation. Receptors for several growth factors, including epidermal growth factor (EGF) and platelet-derived growth factor, contain ligand-activated, tyrosinespecific protein kinase domains essential for biological activity (76, 78). Similarly, the protein products of several oncogenes (e.g., src and ab) exhibit tyrosine kinase activities essential for oncogenic transformation (36,41).The identities of relevant substrates for tyrosine kinases remain largely obscure because of the technical challenge of monitoring transient tyrosine phosphorylation events against high backgrounds of serine/threonine phosphorylation and because of the complex and temporally protracted nature of mitogenesis. Nevertheless, several potential substrates for tyrosine kinases in intact cells have been identified, using combinations of 32p labeling, electrophoresis, phosphoami-* Corresponding author. no acid analysis, and immunoprecipitation and immunoblotting with antiphosphotyrosine (anti-P-Tyr) antibodies. One gro...

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“…The fl and y chains belong to the cytokine receptor family which has no catalytic domain like kinases. IL-2 induced, however, tyrosine phosphorylation of the fl and 7 chains of IL-2R [2,3] and of cellular proteins [4][5][6][7][8], and the IL-2R complex contained tyrosine kinase activity [3,9,10].…”

Section: Introductionmentioning

confidence: 99%

Interleukin 2‐induced activation of JAK3: Possible involvement in signal transduction for c‐myc induction and cell proliferation

et al. 1994

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We have investigated the role of JAK3 in interleukin 2 (IL-2)-induced signal transduction with a human T cell line, ED40515(-), lacking expression of the IL-2 receptor y chain and its sublines transfected with wild-type or mutant cDNAs of the IL-2 receptor y chain. Our results demonstrated that the membrane-proximal cytoplasmic region, encompassing the src homology region 2 (SH2)-like subdomain, of the y chain is essential for association and activation of JAK3. Furthermore, IL-2-induced activation of JAK3 paralleled induction of the c-myc gene and DNA synthesis but not induction of the c-fos and c-jun genes. These results support the hypothesis that JAK3 plays a pivotal role in the IL-2 receptormediated signals for cell growth.

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Interleukin 3 and phorbol ester stimulate tyrosine phosphorylation of overlapping substrate proteins

Cited by 13 publications

References 35 publications

Signal transduction of human interleukin 3 and granulocyte-macrophage colony-stimulating factor through serine and tyrosine phosphorylation

Signal transduction of human interleukin 3 and granulocyte-macrophage colony-stimulating factor through serine and tyrosine phosphorylation

Angiotensin II stimulates protein-tyrosine phosphorylation in a calcium-dependent manner.

Interleukin 2‐induced activation of JAK3: Possible involvement in signal transduction for c‐myc induction and cell proliferation

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