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

Jau‐Song ‐S Yu, Shiaw‐Der ‐D Yang*

*Corresponding author for this work

Research output: Contribution to journalJournal Article peer-review

31 Scopus citations

Abstract

Modulation of protein Kinase F/GSK‐3α by tyrosine phosphorylation in A431 cells was investigated. Kinase F A/GSK‐3α 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 concentration dependent manner by 50‐400 μM genistein( a Specific tyrosine kinase inhibitor), as demonstrated by metobolic 32p‐labeling of the cells followed by immunoprecipitation and two‐dimensional phosphoamino acid analysis and byimmunodetection in an antikinase FA/GSK‐3α immunoprecipitate kinase assay. Taken together, the results provide evidence that Kinase FA/GSK‐3α may exist in a highly tyrosine‐phosphorylated/activated state in resting cells which can by tyrosine‐dephosphorylated and nactivated by extracellular stimulus and that tyrosine kinase(s) and /or tyrosine phosphatase(s) may play a role in the modulation of kinse FA/GSK‐3α activity in cells.

Original languageEnglish
Pages (from-to)131-141
Number of pages11
JournalJournal of Cellular Biochemistry
Volume56
Issue number1
DOIs
StatePublished - 09 1994

Keywords

  • A431 cells
  • genistein
  • inactivation
  • kinase FQGSK‐3α
  • tyrosine dephosphorlation

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