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A more recent version of this article appeared on December 1, 2002
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Submitted on May 2, 2002
Revised on July 10, 2002
Accepted on September 4, 2002
1 Cancer Research UK London Research Institute, Lincoln's Inn Fields Laboratories, Transcription Laboratory, Room 401, 44 Lincoln's Inn Fields, London WC2A 3PX, UK
2 Cancer Research UK London Research Institute, Lincoln's Inn Fields Laboratories, Transcription Laboratory, Room 401, 44 Lincoln's Inn Fields, London WC2A 3PX, UK (present address: INSERM U344, Endocrinologie Moleculaire, 156 Rue de Vaurigard, 75730 Paris Cedex 15, France)
* Corresponding author. E-mail address: Richard.Treisman{at}cancer.org.uk.
Signal-induced activation of the transcription factor SRF (Serum Response Factor) requires alterations in actin dynamics. SRF activity can be inhibited by ectopic expression of ß-actin, either because actin itself participates in SRF regulation or as a consequence of cytoskeletal perturbations. To distinguish between these possibilities, we studied actin mutants. Three mutant actins, G13R, R62D and a C-terminal VP16 fusion protein, were shown not to polymerise in vivo, as judged by two-hybrid, immunofluorescence and cell fractionation studies. These actins effectively inhibited SRF activation, as did wildtype actin, which increased the G-actin level without altering the F:G actin ratio. Physical interaction between SRF and actin was not detectable by mammalian or yeast two-hybrid assays, suggesting that SRF regulation involves an unidentified cofactor. SRF activity was not blocked upon inhibition of CRM1-mediated nuclear export by leptomycin B. Two actin mutants were identified, V159N and S14C, whose expression favoured F-actin formation and which strongly activated SRF in the absence of external signals. These mutants appeared unable to inhibit SRF activity, since their expression did not reduce the absolute level of G-actin as assessed by DNase I binding. Taken together these results provide strong evidence that G-actin, or a subpopulation of it, plays a direct role in signal transduction to SRF.
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