Phospholipase C-gamma, protein kinase C and Ca2+/calmodulin-dependent protein kinase II are involved in platelet-derived growth factor-induced phosphorylation of Tiam1

I N Fleming, C M Elliott, J H Exton

Research output: Contribution to journalArticle

36 Citations (Scopus)

Abstract

In Swiss 3T3 fibroblasts, the Rac1-specific guanine nucleotide exchange factor Tiam1 is phosphorylated by several different agonists. We show here that PDGF induces threonine phosphorylation of Tiam1 in a time- and dose-dependent manner. Tiam1 phosphorylation was significantly reduced by the selective protein kinase C inhibitor Ro-31-8220 and by KN93, an inhibitor of Ca2+/calmodulin-dependent protein kinase II. The Ca2+ chelator BAPTA/AM totally abrogated Tiam1 phosphorylation, indicating that Ca2+ is essential for this phosphorylation. Moreover, PDGF-stimulated Tiam1 phosphorylation was markedly reduced by 72 +/- 10% in PLC-gamma1 deficient mouse fibroblasts, compared to wild-type cells, indicating that phosphoinositide phospholipase C is involved.
Original languageEnglish
Pages (from-to)229-33
Number of pages5
JournalFEBS Letters
Volume429
Issue number3
Publication statusPublished - 1998

Keywords

  • 3T3 Cells
  • Animals
  • Benzylamines
  • Calcium
  • Calcium-Calmodulin-Dependent Protein Kinase Type 2
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Dose-Response Relationship, Drug
  • Egtazic Acid
  • Guanine Nucleotide Exchange Factors
  • Indoles
  • Isoenzymes
  • Mice
  • Phospholipase C gamma
  • Phosphorylation
  • Platelet-Derived Growth Factor
  • Protein Kinase C
  • Proteins
  • Signal Transduction
  • Substrate Specificity
  • Sulfonamides
  • Threonine
  • Type C Phospholipases

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