A protein‐tyrosine kinase in the nuclear matrix from rat liver

Ohmura, Yoshihisa; Teraoka, Hirobumi; Tsukada, Kinji

doi:10.1016/0014-5793(86)81067-5

Cited by 10 publications

(4 citation statements)

References 15 publications

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“…The presence of a 30-kDa tyrosine kinase associated with rat liver NM and capable of autophosphorylation has been reported previously (40,57). We have also detected a single 30-kDa band in our NM preparations by Western blotting with an anti-phosphotyrosine MAb (data not shown), but there is no evidence at present about this 30-kDa protein representing the previously reported tyrosine kinase or about the role that this tyrosine kinase might play in the release of pTP from the NM.…”

Section: Resultssupporting

confidence: 65%

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Tyrosine kinase-dependent release of an adenovirus preterminal protein complex from the nuclear matrix

Angeletti

Engler

1996

J Virol

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Adenovirus (Ad) replicative complexes form at discrete sites on the nuclear matrix (NM) through the interaction of Ad preterminal protein (pTP). The NM is a highly salt-resistant fibrillar network which is known to anchor transcription, mRNA splicing, and DNA replication complexes. Incubation of rATP with NM to which pTP was bound caused the release of pTP as a pTP-NM complex with a size of 220 to 230 kDa; incubation with 5 adenylylimidodiphosphate (rAMP-PNP) showed no significant release, indicating that rATP hydrolysis was required. With NM extracts, it was shown that a pTP-NM complex which was capable of binding Ad origin DNA could be reconstituted in vitro. A number of high-molecular-weight NM proteins ranging in size from 120 to 200 kDa were identified on Far Western blots for their ability to bind pTP. rATP-dependent release of pTP from the NM was inhibited in a dose-dependent fashion by the addition of tyrosine kinase inhibitors, such as quercetin, methyl-2,5-dihydroxycinnamate, or genistein. NM-mediated phosphorylation of a poly(Glu, Tyr) substrate was also significantly abrogated by the addition of these compounds. rATP-dependent release of Ad DNA termini bound to the NM via pTP was also blocked by the addition of these inhibitors. These results indicate that a tyrosine kinase mechanism controls the release of pTP from its binding sites on the NM. These data support the concept that phosphorylation may play a key role in the modulation of pTP binding sites on the NM.

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Section: Resultssupporting

confidence: 65%

“…Rb has also been shown to directly bind lamin A and C (33). There is also evidence of both casein kinase II and tyrosine kinase activity associated with the NM (40,54). We reasoned that these NM kinase activities may play a role in controlling the binding of pTP-NM complexes or pTP itself to the NM in a manner similar to that for other NM proteins.…”

mentioning

confidence: 99%

Tyrosine kinase-dependent release of an adenovirus preterminal protein complex from the nuclear matrix

Angeletti

Engler

1996

J Virol

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“…Thus, c-Abl is a candidate for the insulin-sensitive nuclear tyrosine kinase beside the nuclear insulin receptor. In addition, a protein-tyrosine kinase with a molecular weight of 30 kDa and localized in nuclear matrix of rat liver has been identified (Ohmura et al, 1986). We cannot rule out the possibility that the effects of insulin on the nuclear accumulation of insulin receptors and the stimulation of nuclear tyrosine kinase activity may be due to cross-activation of IGF-1 receptors by insulin.…”

Section: Discussionmentioning

confidence: 95%

Insulin induces rapid accumulation of insulin receptors and increases tyrosine kinase activity in the nucleus of cultured adipocytes

Kim

Kahn

1993

Journal Cellular Physiology

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To better understand the mechanism by which insulin exerts effects on events at the cell nucleus, we have studied insulin receptors and tyrosine kinase activity in nuclei isolated by sucrose density gradient centrifugation following insulin treatment of differentiated 3T3-F442A cells. Insulin stimulated nuclear accumulation of insulin receptors by approximately threefold at 5 min. The half-maximal effect was observed with 1-10 nM insulin. Following insulin treatment, phosphotyrosine content associated with the nuclear insulin receptor was also increased by twofold at 5 min with a similar insulin concentration dependency. These nuclear insulin receptors differ from the membrane-associated insulin receptors in that they were not efficiently solubilized with 1% Triton X-100. During the same period of time, insulin stimulated nuclear tyrosine kinase activity toward the exogenous substrate poly Glu4:Tyr1 tenfold in a time-dependent manner reaching a maximum at 30 min. The insulin receptor substrate protein 1 (IRS-1) could not be detected in the nucleus by immunoblotting. However, a nuclear protein with M(r) approximately 220 kDa was tyrosine phosphorylated, and insulin further stimulated this process threefold > 30 mins. Surface labeling was performed to determine if the nuclear insulin receptors would emerge from the plasma membrane fraction. Using 125I-BPA-insulin with intact cells, the intensity of nuclear insulin receptor labeling was negligible and not increased throughout 30 min incubation at 37 degrees C. In contrast, there was an increase in labeled receptors in the microsomal fraction following insulin treatment. Taken together, these results indicate that insulin rapidly increases nuclear insulin receptor appearance and activates nuclear tyrosine kinase activity. The insulin-induced accumulation of nuclear insulin receptors cannot be accounted for by internalization of surface membrane receptors. These effects of insulin may play an important role in action of the hormone at the nuclear level.

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“…To our knowledge, this is the first report identifying a nuclear-matrix-associated protein tyrosine kinase. A 30 kDa protein kinase that autophosphorylates on tyrosine was reported in the nuclear matrix from rat liver using activity gel assays [34]. The identity of this tyrosine kinase is not known.…”

Section: Discusslonmentioning

confidence: 99%

Association of Lyn Tyrosine Kinase with the Nuclear Matrix and Cell‐Cycle‐Dependent Changes in Matrix‐Associated Tyrosine Kinase Activity

Radha

Nambirajan

Swarup

1996

European Journal of Biochemistry

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The nuclear matrix isolated from HeLa cells and Rat2 fibroblasts harbor? tyrosine kinase and tyrosine phosphatase activities. Polypeptides of 53, 56 and 60 kDa, associated with this subnuclear structure, were phosphorylated at tyrosine in vivo. By immunoblot and immunolabelling experiments, we identified one of the nuclear-matrix-associated tyrosine kinases as Lyn, a Src family member. Lyn was distributed as foci throughout the matrix. The p56 and p53 isoforms of Lyn remained firmly associated with the nuclear matrix after a variety of matrix preparation procedures, and were not detectable in the chromatin fraction of the nucleus. The tyrosine kinase activity associated with the nuclear matrix showed cell-cycle-dependent changes, maximum activity being observed at the G,/S transition phase. Polyoma-virus-transformed rat fibroblast cells showed sixfold higher tyrosine kinase activity in the nuclear matrix preparations compared to that in untransformed cells. These observations are consistent with the suggestion that tyrosine kinase activity associated with the nuclear matrix may be an important determinant of cellular proliferation.Keywords: nuclear matrix ; Lyn tyrosine kinase ; cell cycle ; protein phosphorylation ; nuclear tyrosine kinase.Phosphorylation at tyrosine residues regulates properties of proteins such as enzyme activity, subcellular localization and intermolecular interaction. In eukaryotic cells, this modification effects the response of the cell to its external environment by helping to transmit signals from the cell membrane across the cytoplasm to the nucleus, where actual control of gene expression takes place [I]. The intracellular protein tyrosine kinases (PTKs) and protein tyrosine phosphatases (PTPs) are either associated with various structures such as the plasma membrane, endoplasmic reticulum, cytoskeleton, spindle fibres and mitochondria or are present in a soluble form in the cytoplasm [2, 31. The activities and substrate specificities of these enzymes in vivo are determined by phosphorylation, association with other proteins and subcellular compartmentalization [4, 51.Recent studies have identified the presence of tyrosine-phosphorylated proteins in the nucleus and their role in cell-cycle control and as transcription factors [6, 71. Both cytoplasmic and nuclear proteins are phosphorylated at tyrosine residues in the signalling pathway of mitogenesis. A few tyrosine kinases and phosphatases have been shown to localize to the nucleus, but their physiological functions have not been well defined 13, 81. PTKs known to localize to the nucleus constitutively are Wee 1, Abl, Fer/Fer T and Fgr 181. The Src tyrosine kinase, which is the prototype member of the Src family of kinases, is an ubiqui- tously expressed cytoplasmic enzyme and has been shown to be localized in the nucleus of calcium-induced differentiating keratinocytes 191. Studies on the subnuclear distribution of the tyrosine phosphorylated proteins and the PTKs and PTPs are generally lacking and could provide clues to the role of...

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A protein‐tyrosine kinase in the nuclear matrix from rat liver

Cited by 10 publications

References 15 publications

Tyrosine kinase-dependent release of an adenovirus preterminal protein complex from the nuclear matrix

Tyrosine kinase-dependent release of an adenovirus preterminal protein complex from the nuclear matrix

Insulin induces rapid accumulation of insulin receptors and increases tyrosine kinase activity in the nucleus of cultured adipocytes

Association of Lyn Tyrosine Kinase with the Nuclear Matrix and Cell‐Cycle‐Dependent Changes in Matrix‐Associated Tyrosine Kinase Activity

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