Colchicine Activates Actin Polymerization by Microtubule Depolymerization

Hyo Il Jung, Incheol Shin, Young Mok Park, Ke Won Kang, Kwon Soo Ha

Research output: Contribution to journalArticle

42 Citations (Scopus)

Abstract

Swiss 3T3 fibroblasts were treated with the microtubule-disrupting agent colchicine to study any interaction between microtubule dynamics and actin polymerization. Colchicine increased the amount of filamentous actin (F-actin), in a dose- and time-dependent manner with a significant increase at 1 h by about 130% over control level. Confocal microscopic observation showed that colchicine increased F-actin contents by stress fiber formation without inducing membrane ruffling. Colchicine did not activate phospholipase C and phospholipase D, whereas lysophosphatidic acid did, indicating that colchicine may have a different mechanism of actin polymerization regulation from LPA. A variety of microtubule-disrupting agents stimulated actin polymerization in Swiss 3T3 and Rat-2 fibroblasts as did colchicine, but the microtubule-stabilizing agent taxol inhibited actin polymerization induced by the above microtubule-disrupting agents. In addition, colchicine-induced actin polymerization was blocked by two protein phosphatase inhibitors, okadaic acid and calyculin A. These results suggest that microtubule depolymerization activates stress fiber formation by serine/threonine dephosphorylation in fibroblasts.

Original languageEnglish
Pages (from-to)431-437
Number of pages7
JournalMolecules and cells
Volume7
Issue number3
Publication statusPublished - 1997 Jun 30

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

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    Jung, H. I., Shin, I., Park, Y. M., Kang, K. W., & Ha, K. S. (1997). Colchicine Activates Actin Polymerization by Microtubule Depolymerization. Molecules and cells, 7(3), 431-437.