Bistratene A causes phosphorylation of talin and redistribution of actin microfilaments in fibroblasts: Possible role for PKC-δ

Dianne Watters*, Bernadette Garrone, Geoffrey Gobert, Scott Williams, Robert Gardiner, Martin Lavin

*Corresponding author for this work

Research output: Contribution to journalArticle

29 Citations (Scopus)

Abstract

Bistratene A is a marine toxin which induces phosphorylation of cellular proteins. Our current evidence indicates that this occurs through activation of protein kinase C-δ. In fibroblasts bistratene A causes rounding up of the cells and a rapid disappearance of vinculin staining and actin stress fibers as detected by fluorescence immunohistochemistry. Phosphorylation of the focal adhesion protein, talin, is increased after bistratene A treatment and this is inhibited by calphostin C, a specific inhibitor of PKC. No changes in the phosphorylation status of vinculin, tubulin, or vimentin were observed in the presence of the toxin. Treatment with bistratene A caused a redistribution of PKC-δ from cytosolic and membrane compartments to the nuclear fraction. There was no effect on the subcellular distribution of any other PKC isoform. These results demonstrate that phosphorylation of talin is implicated in the disruption of actin microfilaments in fibroblasts by bistratene A and that this is most likely mediated by PKC-δ.

Original languageEnglish
Pages (from-to)327-335
Number of pages9
JournalExperimental Cell Research
Volume229
Issue number2
DOIs
Publication statusPublished - 15 Dec 1996
Externally publishedYes

ASJC Scopus subject areas

  • Cell Biology

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