PP1/PP2A phosphatases inhibitors okadaic acid and calyculin A block ERK5 activation by growth factors and oxidative stress

Lourdes Garcia, Fatima Garcia, Franc Llorens, Mercedes Unzeta, Emilio Itarte, Néstor Gómez

Research output: Contribution to journalArticleResearchpeer-review

41 Citations (Scopus)

Abstract

Okadaic acid is an inhibitor of the protein Ser/Thr phosphatases PP1 and PP2A, which blocks the activation of extracellular signal-regulated protein kinase 5 (ERK5), a member of the MAP kinase family activated by growth factors and several types of stressors. The blocking of ERK5 activation by okadaic acid was observed in HeLa cells exposed to epidermal growth factor and H2O2 as well as in PC12 cells stimulated by nerve growth factor and H2O2. Calyculin A, another PP1 and PP2A inhibitor, behaved similarly although these compounds are not structurally related. This suggests that either PP1 or PP2A or both are necessary for ERK5 activation. Protein kinase C (PKC) acts as a negative regulator of the ERK5 activation pathway, however our data suggest that the effects of PKC and the phosphatase are unrelated. © 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
Original languageEnglish
Pages (from-to)90-94
JournalFEBS Letters
Volume523
Issue number1-3
DOIs
Publication statusPublished - 17 Jul 2002

Keywords

  • Calyculin A
  • Epidermal growth factor
  • Extracellular signal-regulated protein kinase 5
  • Okadaic acid
  • Protein kinase C

Fingerprint Dive into the research topics of 'PP1/PP2A phosphatases inhibitors okadaic acid and calyculin A block ERK5 activation by growth factors and oxidative stress'. Together they form a unique fingerprint.

Cite this