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

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

    Research output: Contribution to journalArticle

    6 Citations (Scopus)

    Abstract

    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.

    Original languageEnglish
    Pages (from-to)207-212
    Number of pages6
    JournalArchives of Biochemistry and Biophysics
    Volume413
    Issue number2
    DOIs
    Publication statusPublished - 2003 May 15

    Keywords

    • Btk29A
    • Drosophila
    • Phosphoglucomutase
    • Tyrosine kinase
    • Tyrosine phosphorylation

    ASJC Scopus subject areas

    • Biochemistry
    • Biophysics
    • Molecular Biology

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