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Tyrosin dephosphorylation and concurrent inactivation of protein kinase FA/GSK-3α by genistein in A431 cells

✍ Scribed by Jau-Song Yu; Shiaw-Der Yang

Publisher
John Wiley and Sons
Year
1994
Tongue
English
Weight
1020 KB
Volume
56
Category
Article
ISSN
0730-2312

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✦ Synopsis

Modulation of protein kinase FA/GSK-3a by tyrosine phosphorylation in A431 cells was investigated. Kinase F A / G S K -~~ was found to exist in a highly tyrosine-phosphorylated/activated state in resting cells but could become tyrosine-dephosphorylated and inactivated down to less than 30% of control values in a concentrationdependent manner by 50-400 pM genistein (a specific tyrosine kinase inhibitor), as demonstrated by metabolic 32P-labeling of the cells followed by immunoprecipitation and two-dimensional phosphoamino acid analysis and by immunodetection in an antikinase FA/GSK-3a immunoprecipitate kinase assay. Taken together, the results provide evidence that kinase FA/GSK-3a may exist in a highly tyrosine-phosphorylated/activated state in resting cells which can be tyrosine-dephosphorylated and inactivated by extracellular stimulus and that tyrosine kinase(s) and/or tyrosine phosphatase(s) may play a role in the modulation of kinase FA/GSK-3a activity in cells.

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