Casein Kinase 2 (CK2)-Mediated Reduction of the Activities of Src Family Tyrosine Kinases in Vitro(Biochemistry/Molecular Biology)
スポンサーリンク
概要
- 論文の詳細を見る
The physiological correlation between casein kinase 2 (CK2) and two Src family tyrosine kinases (Src-TKs, Fyn and Src) was mainly investigated in vitro. It was found that (i) Thr-residues of these two Src-TKs were preferentially phosphorylated by CK2 using [γ-^<32>P]GTP as a phosphate donor ; (ii) this phosphorylation was highly stimulated in the presence of poly-Arg ; (iii) full phosphorylation of two Src-TKs by CK2 resulted in significant reduction of their TK activities ; and (iv) quercetin (a CK2 inhibitor) inhibited the CK2-mediated reduction of their Src-TK activities in vitro. Under the same experimental conditions, similar results were obtained with Yes. These results suggest that CK2 may be a protein kinase responsible for the suppression of at least three Src-TKs (Fyn, Src and Yes) through the specific phosphorylation of their Thr-residues at the cellular level.
- 2004-12-01
著者
-
Kamata Yayoi
Genetical Biochemistry And Signal Biology Graduate School Of Medical Sciences Kitasato University
-
Ohtsuki Kenzo
Genetical Biochem. Kitasato Univ.
-
Ohtsuki Kenzo
Genetical Biochemistry And Signal Biology Graduate School Of Medical Sciences Kitasato University
-
YOKOYAMA Takamasa
Genetical Biochemistry and Signal Biology, Graduate School of Medical Sciences, Kitasato University
-
Yokoyama Takamasa
Genetical Biochemistry And Signal Biology Graduate School Of Medical Sciences Kitasato University
-
KAMATA Yayoi
Genetical Biochemistry and Signal Biology, Graduate School of Medical Sciences, Kitasato University
-
OHTSUKI Kenzo
Genetical Biochemistry and Signal Biology, Graduate School of Medical Sciences, Kitasato University
関連論文
- A Novel Consensus Phosphorylation Motif in Sulfatide- and Cholesterol-3-sulfate-Binding Protein Substrates for CK1 in Vitro(Biochemistry)
- Casein Kinase 2 (CK2)-Mediated Reduction of the Activities of Src Family Tyrosine Kinases in Vitro(Biochemistry/Molecular Biology)
- Casein Kinase II (CK-II)-Mediated Stimulation of HIV-1 Reverse Transcriptase Activity and Characterization of Selective Inhibitors in Vitro
- Biochemical Characterization of Recombinant HIV-1 Reverse Transcriptase (rRT) as a Glycyrrhizin-Binding Protein and the CK-II-Mediated Stimulation of rRT Activity Potently Inhibited by Glycyrrhetinic Acid Derivative
- Biochemical Characterization of 60S Acidic Ribosomal P Proteins Associated with CK-II from Bamboo Shoots and Potent Inhibitors of Their Phosphorylation in Vitro
- Activation of C-Kinase η through Its Cholesterol-3-sulfate-Dependent Phosphorylation by Casein Kinase I in Vitro(Biochemistry/Molecular Biology)
- Characterization of (-)-Matairesinol as a Potent Inhibitor of Casein Kinase I in Vitro
- BIOCHEMICAL CHARACTERIZATION OF A 56 kDa DNABINDING PROTEIN(p56)PURIFIED FROM THE SPINACH CHLOROPLAST FRACTION AS AN EFFECTIVE PHOSPHATE ACCEPTOR FOR CASEIN KINASE II (CK-II)
- Chloroplast Ribonucleoproteins (RNPs) as Phosphate Acceptors for Casein Kinase II : Purification by ssDNA-Cellulose Column Chromatography : PROTEINS, ENZYMES AND METABOLISM
- Further Characterization of Galloyl Pedunculagin as an Effective Autophosphorylation Inhibitor of C-Kinase in Vitro
- Characterization of Bovine Angiogenin-1 and Lactogenin-Like Protein as Glycyrrhizin-Binding Proteins and Their in Vitro Phosphorylation by C-kinase
- Characterization of Bovine and Human Lactoferrins as Glycyrrhizin-Binding Proteins and Their Phosphorylation in Vitro by Casein Kinase II
- Biochemical Characterization of Bovine Lactoferrin as a Glycyrrhizin-Binding Protein in Vitro
- Biochemical Characterization of Phospholipids, Sulfatide and Heparin as Potent Stimulators for Autophosphorylation of GSK-3β and the GSK-3β-Mediated Phosphorylation of Myelin Basic Protein In vitro
- Biochemical Characterization of Galloyl Pedunculagin (Ellagitannin) as a Selective Inhibitor of the β-Regulatory Subunit of A-Kinase In Vitro
- Characterization of Complement C3 as a Glycyrrhizin (GL)-Binding Protein and the Phosphorylation of C3a by CK-2, Which Is Potently Inhibited by GL and Glycyrrhetinic Acid In Vitro
- Biochemical Characterization of Suramin as a Selective Inhibitor for the PKA-Mediated Phosphorylation of HBV Core Protein in Vitro(Biochemistry)
- BIOLOGICAL SIGNIFICANCE OF THE CASEINKINASE II (CK-II) CATALYZED PHOSPHORYLATION OF 34 kDaRIBONUCLEOPROTEIN (p34) IN CHLOROPLAST POST TRANSCRIPTIONALREGULATION
- Purification and Characterization of Three Distinct Protein Kinases from Marchantia polymorpha