Biochemical characterization of a casein kinase I-like actin kinase responsible for the actin-induced suppression of casein kinase II activity in vitro

Atsushi Karino, Maiko Okano, Masahito Hatomi, Takeshi Nakamura, Kenzo Ohtsuki

研究成果: ジャーナルへの寄稿記事

8 引用 (Scopus)

抄録

By combination of column chromatographies (heparin-agarose, HiTrap heparin and HiTrap SP columns) and gel filtration on a Superdex 200-pg HPLC column, an actin kinase was partially purified from a 1.5 M NaCl extract of porcine liver. The actin kinase was finally purified, by actin-Sepharose column chromatography (HPLC), as an actin-binding protein kinase. The biochemical properties, such as (1) requirements of divalent cations (10 mM Mg2+ and 3 mM Mn2+) and effective phosphate acceptors (actin and α-casein), (2) phosphorylation of both Ser- and Thr-residues on these two phosphate acceptors, (3) autophosphorylation of the catalytic subunit (approximately 37 kDa), and (4) inhibition kinetics by CK-I-7 (a CK-I specific inhibitor), of the purified actin kinase were similar to those reported for CK-I purified from various mammalian cells, but it was distinguishable from three cellular actin kinases (A-kinase, C-kinase and actin-fragmin kinase (approximately 80 kDa)). The 37 kDa actin kinase-mediated phosphorylation of actin did not relate to its polymerizability. Inhibition of CK-II-mediated phosphorylation of functional cellular proteins, including calmodulin (CaM), by actin was significantly stimulated after its full phosphorylation by the purified 37 kDa actin kinase or rCK-I in vitro. These results suggest that: (1) the 37 kDa Ser/Thr actin-binding kinase may be classified as a member of the CK-I family; and (2) specific phosphorylation of actin by the actin kinase may be involved in the suppression mechanism of CK-II-mediated signal transduction at the cellular level. Copyright (C) 1999 Elsevier Science B.V.

元の言語英語
ページ(範囲)603-616
ページ数14
ジャーナルBiochimica et Biophysica Acta - General Subjects
1472
発行部数3
DOI
出版物ステータス出版済み - 11 16 1999

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Casein Kinase I
Casein Kinase II
Actins
Phosphorylation
Column chromatography
Phosphotransferases
Phosphates
High Pressure Liquid Chromatography
Microfilament Proteins
Signal transduction
actin kinase
In Vitro Techniques
Liver Extracts
Agarose Chromatography
Divalent Cations
Calmodulin
Caseins
Liver
Sepharose
Protein Kinases

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology

これを引用

Biochemical characterization of a casein kinase I-like actin kinase responsible for the actin-induced suppression of casein kinase II activity in vitro. / Karino, Atsushi; Okano, Maiko; Hatomi, Masahito; Nakamura, Takeshi; Ohtsuki, Kenzo.

:: Biochimica et Biophysica Acta - General Subjects, 巻 1472, 番号 3, 16.11.1999, p. 603-616.

研究成果: ジャーナルへの寄稿記事

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abstract = "By combination of column chromatographies (heparin-agarose, HiTrap heparin and HiTrap SP columns) and gel filtration on a Superdex 200-pg HPLC column, an actin kinase was partially purified from a 1.5 M NaCl extract of porcine liver. The actin kinase was finally purified, by actin-Sepharose column chromatography (HPLC), as an actin-binding protein kinase. The biochemical properties, such as (1) requirements of divalent cations (10 mM Mg2+ and 3 mM Mn2+) and effective phosphate acceptors (actin and α-casein), (2) phosphorylation of both Ser- and Thr-residues on these two phosphate acceptors, (3) autophosphorylation of the catalytic subunit (approximately 37 kDa), and (4) inhibition kinetics by CK-I-7 (a CK-I specific inhibitor), of the purified actin kinase were similar to those reported for CK-I purified from various mammalian cells, but it was distinguishable from three cellular actin kinases (A-kinase, C-kinase and actin-fragmin kinase (approximately 80 kDa)). The 37 kDa actin kinase-mediated phosphorylation of actin did not relate to its polymerizability. Inhibition of CK-II-mediated phosphorylation of functional cellular proteins, including calmodulin (CaM), by actin was significantly stimulated after its full phosphorylation by the purified 37 kDa actin kinase or rCK-I in vitro. These results suggest that: (1) the 37 kDa Ser/Thr actin-binding kinase may be classified as a member of the CK-I family; and (2) specific phosphorylation of actin by the actin kinase may be involved in the suppression mechanism of CK-II-mediated signal transduction at the cellular level. Copyright (C) 1999 Elsevier Science B.V.",
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T1 - Biochemical characterization of a casein kinase I-like actin kinase responsible for the actin-induced suppression of casein kinase II activity in vitro

AU - Karino, Atsushi

AU - Okano, Maiko

AU - Hatomi, Masahito

AU - Nakamura, Takeshi

AU - Ohtsuki, Kenzo

PY - 1999/11/16

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N2 - By combination of column chromatographies (heparin-agarose, HiTrap heparin and HiTrap SP columns) and gel filtration on a Superdex 200-pg HPLC column, an actin kinase was partially purified from a 1.5 M NaCl extract of porcine liver. The actin kinase was finally purified, by actin-Sepharose column chromatography (HPLC), as an actin-binding protein kinase. The biochemical properties, such as (1) requirements of divalent cations (10 mM Mg2+ and 3 mM Mn2+) and effective phosphate acceptors (actin and α-casein), (2) phosphorylation of both Ser- and Thr-residues on these two phosphate acceptors, (3) autophosphorylation of the catalytic subunit (approximately 37 kDa), and (4) inhibition kinetics by CK-I-7 (a CK-I specific inhibitor), of the purified actin kinase were similar to those reported for CK-I purified from various mammalian cells, but it was distinguishable from three cellular actin kinases (A-kinase, C-kinase and actin-fragmin kinase (approximately 80 kDa)). The 37 kDa actin kinase-mediated phosphorylation of actin did not relate to its polymerizability. Inhibition of CK-II-mediated phosphorylation of functional cellular proteins, including calmodulin (CaM), by actin was significantly stimulated after its full phosphorylation by the purified 37 kDa actin kinase or rCK-I in vitro. These results suggest that: (1) the 37 kDa Ser/Thr actin-binding kinase may be classified as a member of the CK-I family; and (2) specific phosphorylation of actin by the actin kinase may be involved in the suppression mechanism of CK-II-mediated signal transduction at the cellular level. Copyright (C) 1999 Elsevier Science B.V.

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