SPECIFIC DETECTION OF AN INTERLEUKIN 1- AND TUMOUR NECROSIS FACTOR- ACTIVATED β-CASEIN KINSASE IN HeLa AND KB CELLS

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

doi:10.1006/cyto.1996.0190

Cited by 5 publications

(18 citation statements)

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“…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: 96%

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: Isolation Purification and Cloning Of Human Nek8 Andmentioning

confidence: 96%

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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“…IL1 and TNF also activate protein kinases which are not associated with the receptors and do not belong to the MAPK pathways (10,(23)(24)(25)(26)(27). One of them was detected by virtue of its ability to phosphorylate in vitro the bovine milk protein, ␤ casein, and was originally termed ␤ casein kinase (10,26,27).…”

mentioning

confidence: 99%

“…One of them was detected by virtue of its ability to phosphorylate in vitro the bovine milk protein, ␤ casein, and was originally termed ␤ casein kinase (10,26,27). The chromatographic properties of ␤ casein kinase and its inability to phosphorylate ␣ casein (10) distinguish it from casein kinase 1 (CK1) and casein kinase 2 (CK2), two ubiquitous protein kinases that also owe their names to their ability to phosphorylate caseins in vitro (28).…”

mentioning

confidence: 99%

“…In contrast to the MAPK pathways, ␤ casein kinase is not activated by mitogens, cellular stresses, or cytokines other than IL1 and TNF (26). To refer to this highly specific regulation and to avoid the confusing term "casein kinase," it has recently been renamed TNF/IL1-activated protein (TIP) kinase (27).…”

mentioning

confidence: 99%

“…TIP kinase is a cytosolic enzyme of about 100 kDa that may be part of larger aggregates of 200 -600 kDa in vivo (10,26,27). Its physiological substrates are unknown.…”

mentioning

confidence: 99%

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Dual Specificity of the Interleukin 1- and Tumor Necrosis Factor-activated β Casein Kinase

Guesdon

Knight²,

Rawlinson³

et al. 1997

Journal of Biological Chemistry

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Tumor necrosis factor (TNF) and interleukin 1 (IL1) activate a protein kinase, TIP kinase, which phosphorylates ␤ casein in vitro. We have now identified its main phosphorylation site on ␤ casein, Ser 124 (K m Ϸ 28 M), and a minor phosphorylation site, Ser 142 (K m Ϸ 0.7 mM). The sequence motif that determined the phosphorylation of Ser 124 by the kinase was studied with synthetic peptides bearing deletions or substitutions of the neighboring residues. This allowed synthesis of improved substrates (K m Ϸ 6 M) and showed that efficient phosphorylation of Ser 124 was favored by the presence of large hydrophobic residues at positions ؉1, ؉9, ؉11, and ؉13 (counted relative to the position of the phosphoacceptor amino acid) and of a cysteine at position ؊2. Peptides in which Ser124 was replaced by tyrosine were also phosphorylated by TIP kinase, showing it to have dual specificity. It is unable to phosphorylate the MAP kinases in vitro and is therefore not directly involved in their activation. Its biochemical characteristics indicate that TIP kinase is a novel dual specificity kinase, perhaps related to the mixed lineage kinases. It copurified with a phosphoprotein of about 95 kDa, which could correspond either to the autophosphorylated kinase or to an associated substrate.

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TNF receptor subtype signalling: Differences and cellular consequences

MacEwan

2002

Cellular Signalling

555

410

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SPECIFIC DETECTION OF AN INTERLEUKIN 1- AND TUMOUR NECROSIS FACTOR- ACTIVATED β-CASEIN KINSASE IN HeLa AND KB CELLS

Cited by 5 publications

References 0 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

Dual Specificity of the Interleukin 1- and Tumor Necrosis Factor-activated β Casein Kinase

TNF receptor subtype signalling: Differences and cellular consequences

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