Phospholipase D is not involved in Rho A-mediated activation of stress fiber formation

Sun Hee Leem, Incheol Shin, Soo Mi Kweon, Seung Il Kim, Jae Hong Kim, Kwon Soo Ha

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)


In order to investigate the role of a small GTP-binding protein RhoA in lysophosphatidic acid (LPA)-induced stress fiber formation, C3 ADP-ribosyltransferase was prepared by expressing in E. coli and then applied to Rat-2 fibroblasts. C3 transferase isolated from E. coli was as effective as the toxin from Clostridium botulinum in ADP-ribosylation of RhoA. Incubation of the cells with C3 transferase for 2 days induced ADP-ribosylation of RhoA by a dose-dependent manner, with a sub-maximal induction at 25 μg/ml. As expected, LPA-induced stress fiber formation was completely blocked by pre-incubation with C3 transferase for 2 days. However, exogenously added C3 transferase had no significant effect on the formation of phosphatidylethanol by LPA. These results suggested that phospholipase D was not activated by RhoA in the LPA-induced stress fiber formation.

Original languageEnglish
Pages (from-to)337-341
Number of pages5
JournalJournal of Biochemistry and Molecular Biology
Issue number5
Publication statusPublished - 1997 Sept 30
Externally publishedYes


  • C3 transferase
  • Lysophosphatidic acid
  • Phospholipase D
  • RhoA
  • Stress fibers

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


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