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Vol. 13, Issue 12, 4167-4178, December 2002
Cancer Research UK London Research Institute, Lincoln's Inn Fields
Laboratories, Transcription Laboratory, London WC2A 3PX, United Kingdom
Signal-induced activation of the transcription factor serum
response factor (SRF) requires alterations in actin dynamics. SRF
activity can be inhibited by ectopic expression of 
-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
polymerize in vivo, as judged by two-hybrid, immunofluorescence, and
cell fractionation studies. These actins effectively inhibited SRF
activation, as did wild-type 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 favored F-actin formation and which strongly
activated SRF in the absence of external signals. These mutants seemed
unable to inhibit SRF activity, because 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.
Cancer Research UK London Research Institute
comprises the Lincoln's Inn Fields and Clare Hall Laboratories of the
former Imperial Cancer Research Fund after the merger of the Imperial Cancer Research Fund with the Cancer Research Campaign in February 2002.
Corresponding author. E-mail address:
richard.treisman{at}cancer.org.uk.
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