Enhanced phosphorylation and enzymatic activity of phosphoglucomutase by the Btk29A tyrosine kinase in Drosophila

Hiroko Inoue, Shunzo Kondo, Yoshimi Hinohara, Naoto Juni, Daisuke Yamamoto

    研究成果: Article

    6 引用 (Scopus)

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    The Drosophila Btk29A tyrosine kinase is suggested to be involved in diverse processes, although its target proteins are unknown. In the present study, we investigated substrates of Btk29A tyrosine kinase by expressing a catalytically activated form of Btk29A-P1 (Btk-EG) in Drosophila compound eyes. Expression in eye disks led to the development of the rough-eye phenotype and increased tyrosine phosphorylation of a 65-kDa protein. Partial amino acid sequence analysis of this protein showed that it was phosphoglucomutase. Phosphoglucomutase activity in heads from Btk-EG-expressing flies was higher than that in controls, suggesting that the levels of tyrosine phosphorylation and activity of the enzyme are associated with Btk29A tyrosine kinase activity.

    元の言語English
    ページ(範囲)207-212
    ページ数6
    ジャーナルArchives of Biochemistry and Biophysics
    413
    発行部数2
    DOI
    出版物ステータスPublished - 2003 5 15

    ASJC Scopus subject areas

    • Biochemistry
    • Biophysics
    • Molecular Biology

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