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

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

*この研究の対応する著者

    研究成果: Article査読

    6 被引用数 (Scopus)

    抄録

    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.

    本文言語English
    ページ(範囲)207-212
    ページ数6
    ジャーナルArchives of Biochemistry and Biophysics
    413
    2
    DOI
    出版ステータスPublished - 2003 5 15

    ASJC Scopus subject areas

    • 生化学
    • 生物理学
    • 分子生物学

    フィンガープリント

    「Enhanced phosphorylation and enzymatic activity of phosphoglucomutase by the Btk29A tyrosine kinase in Drosophila」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

    引用スタイル