Direct Evidence for In Vivo Reversible Tyrosine Phosphorylation of the N-Terminal Domain of the H/K-ATPase .ALPHA.-Subunit in Mammalian Stomach Cells.

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概要

• 論文の詳細を見る

• In vivo reversible phosphorylation of Tyr-7 and Tyr-10 of the pig stomach H/K-ATPase α-chain was initially demonstrated in mammals, rat, rabbit, and pig, in the presence of vanadate+H2O2. In vitro phosphorylation has also been unequivocally demonstrated via the use of protease inhibitors during membrane H/K-ATPase preparation. An amphoretic detergent permitted each intrinsic kinase to phosphorylate each fusion protein containing the requisite Tyr residues, along with a reduction in α-chain phosphorylation. These and other data suggest that some important enzyme systems are present in the apical membrane and that they are in sufficient proximity to participate in the reversible phosphorylation of the amino terminal soluble domain of the α-chain with an unknown physiological function in the membrane embedded H/K-ATPase.

• 社団法人 日本生化学会の論文

著者

• IMAGAWA Toshiaki

  Biological Chemistry, Division of Chemistry, Faculty of Science, Hokkaido University

• SHIMADA Akira

  Biological Chemistry, Graduate School of Science, Hokkaido University

• Mardh Sven

  Department Of Biomedicine And Surgery Faculty Of Science Linkoping University

• Togawa Katsuhiko

  Biological Chemistry Graduate School Of Science Hokkaido University

• Kaya Shunji

  Biological Chemistry Graduate School Of Science Hokkaido University

• Kanagawa Motoi

  Biological Chemistry Graduate School Of Science Hokkaido University

• Taniguchi Kazuya

  Biological Chemistry Graduate School Of Science Hokkaido University

• Watanabe Shunsuke

  Biological Chemistry Graduate School Of Science Hokkaido University

• Umezu Hideki

  Biological Chemistry, Graduate School of Science, Hokkaido University

• Imagawa Toshiaki

  Biological Chemistry, Graduate School of Science, Hokkaido University

関連論文

• New Evidence for ATP Binding Induced Catalytic Subunit Interactions in Pig Kidney Na/K-ATPase
• Evidence for a Relationship between Activity and the Tetraprotomeric Assembly of Solubilized Pig Gastric H/K-ATPase
• The Oligomeric Nature of Na/K-Transport ATPase
• Direct Evidence for In Vivo Reversible Tyrosine Phosphorylation of the N-Terminal Domain of the H/K-ATPase α-Subunit in Mammalian Stomach Cells
• ATP-Induced Dynamic Fluorescence Changes of a N - [ p- (2-Benzimidazolyl)Phenyl] maleimide Probe at Cys^ in the α-Chain of Pig Stomach H^+, K^+-ATPase^1
• Fluorescein 5'-Isothiocyanate-Modified Na^+, K^+-ATPase, at Lys-501 of the α-Chain, Accepts ATP Independent of Pyridoxal 5'-Diphospho-5'-Adenosine Modification at Lys-480^1
• Direct Evidence for In Vivo Reversible Tyrosine Phosphorylation of the N-Terminal Domain of the H/K-ATPase .ALPHA.-Subunit in Mammalian Stomach Cells.

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