Specific activation of <i>β</i>-casein kinase by the inflammatory cytokines interleukin 1 and tumour necrosis factor

Guesdon, François; Waller, R J; Saklatvala, Jeremy

doi:10.1042/bj3040761

Cited by 21 publications

(22 citation statements)

References 33 publications

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“…The identification of Nek8 was based on a search for an IL-1 mediated ␤-casein kinase activity reported by Guesdon et al (21,22). Although we identified Nek8 activity in a homogenate from IL-1-treated rabbits that was absent in homogenates from naïve rabbits, we do not believe that Nek8 corresponds to the previously described activity.…”

Section: Discussionmentioning

confidence: 72%

“…Previous studies had reported the identification of a specific ␤-casein phosphorylating activity induced by IL-1, named ␤-casein kinase (21)(22)(23). This novel activity was shown to be specific for phosphorylating ␤-casein and not ␣-casein, and was distinct from any known mitogen-activated protein kinase or hsp27 kinase.…”

Section: Isolation Purification and Cloning Of Human Nek8 Andmentioning

confidence: 99%

“…Nek8 Is Not Regulated by IL-1-The isolation and purification of Nek8 was originally undertaken to identify a previously described novel ␤-casein kinase activity induced specifically by IL-1 (21,22). Nek8 was subsequently cloned based on tryptic peptide sequence obtained from purified fraction 12 containing IL-1 induced ␤-casein kinase activity.…”

Section: Nek8 Is a Novel Nima-related Kinasementioning

confidence: 99%

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Purification, Cloning, and Characterization of Nek8, a Novel NIMA-related Kinase, and Its Candidate Substrate Bicd2

Holland

Milne

Garka

et al. 2002

Journal of Biological Chemistry

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We describe the isolation, cloning, and characterization of human Nek8, a new mammalian NIMA-related kinase, and its candidate substrate Bicd2. Nek8 was isolated as a ␤-casein kinase activity in rabbit lung and has an N-terminal catalytic domain homologous to the Nek family of protein kinases. Nek8 also contains a central domain with homology to RCC1, a guanine nucleotide exchange factor for the GTPase Ran, and a C-terminal coiled-coil domain. Like Nek2, Nek8 prefers ␤-casein over other exogenous substrates, has shared biochemical requirements for kinase activity, and is capable of autophosphorylation and oligomerization. Nek8 activity is not cell cycle regulated, but like Nek3, levels are consistently higher in G 0 -arrested cells. During the purification of Nek8 a second protein co-chromatographed with Nek8 activity. This protein, Bicd2, is a human homolog of the Drosophila protein Bicaudal D, a coiled-coil protein. Bicd2 is phosphorylated by Nek8 in vitro, and the endogenous proteins associate in vivo. Bicd2 localizes to cytoskeletal structures, and its subcellular localization is dependent on microtubule morphology. Treatment of cells with nocodazole leads to dramatic reorganization of Bicd2, and correlates with Nek8 phosphorylation. This may be indicative of a role for Nek8 and Bicd2 associated with cell cycle independent microtubule dynamics.Among the multiple families of related protein kinases that have been described, the mammalian NIMA related kinases, or Neks, have proven to be elusive in their functional characterization. For the most part, the relatedness of these kinases is restricted to sequence homology within the catalytic domain, as none of the Neks appear to be functionally related to NIMA.

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Section: Discussionmentioning

confidence: 72%

Section: Isolation Purification and Cloning Of Human Nek8 Andmentioning

confidence: 99%

Section: Nek8 Is a Novel Nima-related Kinasementioning

confidence: 99%

See 1 more Smart Citation

Purification, Cloning, and Characterization of Nek8, a Novel NIMA-related Kinase, and Its Candidate Substrate Bicd2

Holland

Milne

Garka

et al. 2002

Journal of Biological Chemistry

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“…However, it has been demonstrated that late displacement of IL-1 from the type I receptor blocks transcription, suggesting that the continued presence of IL-1 on the IL-1RI is critical to amplification of IL-1-mediated biologic effects (26). While most intracellular effects of IL-1 occur rapidly and are short-lived, at least one potential mediator of IL-1 activity with sustained activity was described by Guesdon and coworkers, who demonstrated the persistent presence of active p-casein kinase (47). Transcriptional results mediated by this pathway have not yet been fully defined.…”

Section: Findings Of Western Blot Analysis Of Nf-kbmentioning

confidence: 99%

Involvement of nuclear factor kB in the regulation of cyclooxygenase‐2 expression by interleukin‐1 in rheumatoid synoviocytes

Crofford

Teng

McCarthy

et al. 1997

Arthritis & Rheumatism

242

165

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Objective. To evaluate involvement of the transcription factor nuclear factor KB (NF-KB) in the increased expression of cyclooxygenase-2 (COX-2) stimulated by interleukin-lp (IL-1p) in primary rheumatoid synoviocytes.Methods. We treated early-passage rheumatoid synoviocytes with IL-lp and examined the time course of NF-KB translocation to the nucleus by Western blot analysis, as well as NF-KB binding to the COX-2 promoter/enhancer by electrophoretic mobility shift assay. We correlated the time course of NF-KB binding with expression of COX-2 messenger RNA (mRNA) and protein. Synoviocytes were then treated with either sense or antisense phosphorothioate-modified oligonucleotides derived from the transcription start site of the human NF-KB p65 RNA. We analyzed NF-KB binding to the COX-2 promoter and COX-2 protein levels after these treatments.Results. IL-1p rapidly stimulated the translocation of the p65, p50, and c-re1 NF-KB subunits from the cytoplasm to the nucleus. Electrophoretic mobility shift assay demonstrated binding to 2 NF-KB sites within the COX-2 promoter/enhancer, with a time course identical to that of nuclear localization of NF-KB. Supershift analysis revealed that binding activity was due primarily to the p65-p50 heterodimer and the p50 homodimer. Submitted for publication June 7, 1996; accepted in revised form August 21, 1996. mRNA and protein were increased. Pretreatment of RA synoviocytes with NF-KB p65 antisense oligonucleotides resulted in decreased binding to the COX-2 promoter and decreased COX-2 protein expression.Conclusion. These data demonstrate that signaling via the NF-KB pathway is involved in regulation of COX-2 expression induced by IL-1p in RA synoviocytes.

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“…However, little definitive data have come forth delineating the post-receptor molecular events. TNF receptors do not contain an intrinsic kinase domain, and recently, the involvement of serine/threonine protein kinases, including the so-called mitogen-activated protein kinases (MAPKs), has been proposed by a number of investigators (13)(14)(15)(16)(17). MAPKs form a large family of serine/threonine protein kinases activated by separate cascades and are important mediators of signal transduction from the cell surface to the nucleus.…”

mentioning

confidence: 99%

Tumor Necrosis Factor-α Induces Interleukin-6 Production and Integrin Ligand Expression by Distinct Transduction Pathways

Cesaris

Starace

Riccioli

et al. 1998

Journal of Biological Chemistry

109

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Tumor necrosis factor-␣ (TNF-␣) is a pleiotropic cytokine that elicits a large number of biological effects. However, the intracellular signaling mechanisms that are responsible for the TNF-␣ effects remain largely unknown. We have previously demonstrated that cultured mouse Sertoli cells, after TNF-␣ treatment, increase the surface expression of adhesion molecules such as intercellular adhesion molecule-1 (ICAM-1) and vascular cell adhesion molecule-1 (VCAM-1) and interleukin-6 (IL-6) production (Riccioli, A., Filippini, A., De Cesaris, P., Barbacci, E., Stefanini, M., Starace, G., and Ziparo, E. (1995) Proc. Natl. Acad. Sci. U.S.A. 92, 5808 -5812). Here, we show that, in cultured Sertoli cells, TNF-␣ activates the mitogen-activated protein kinase pathway (p38, cJun N-terminal protein kinase/stress-activated protein kinase, and the p42/p44 mitogen-activated protein kinases) as revealed by an increased phosphorylation of p38, activating transcription factor-2, c-Jun, and Elk-1. Furthermore, our data indicate that the biological effects induced by TNF-␣ in Sertoli cells (enhancement of ICAM-1, VCAM-1, and IL-6 expression) depend on the activation of different signaling pathways. SB203580, a highly specific p38 inhibitor, does not affect ICAM-1 and VCAM-1 expression, but strongly inhibits IL-6 production. Moreover, interferon-␥, which up-regulates adhesion molecule expression and reduces IL-6 production, does not induce phosphorylation of p38. Our data strongly support the hypothesis that, in response to TNF-␣, activation of p38 leads to IL-6 production, whereas ICAM-1 and VCAM-1 expression could be induced by activation of the c-Jun N-terminal protein kinase/stress-activated protein kinase pathway.

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Specific activation of β-casein kinase by the inflammatory cytokines interleukin 1 and tumour necrosis factor

Cited by 21 publications

References 33 publications

Purification, Cloning, and Characterization of Nek8, a Novel NIMA-related Kinase, and Its Candidate Substrate Bicd2

Purification, Cloning, and Characterization of Nek8, a Novel NIMA-related Kinase, and Its Candidate Substrate Bicd2

Involvement of nuclear factor kB in the regulation of cyclooxygenase‐2 expression by interleukin‐1 in rheumatoid synoviocytes

Tumor Necrosis Factor-α Induces Interleukin-6 Production and Integrin Ligand Expression by Distinct Transduction Pathways

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