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Vol. 13, Issue 11, 4088-4099, November 2002
SRF-dependent transcription is regulated by the small GTPase RhoA
via its effects on actin dynamics. The diaphanous-related formin (DRF)
proteins have been identified as candidate RhoA effectors mediating
signaling to SRF. Here we investigate the relationship between SRF
activation and actin polymerization by the DRF mDia1. We show that the
ability of mDia1 to potentiate SRF activity is strictly correlated with
its ability to promote F-actin assembly. Both processes can occur
independently of the mDia1 FH1 domain but require sequences in an
extended C-terminal region encompassing the conserved FH2 domain.
mDia-mediated SRF activation, but not F-actin assembly, can be blocked
by a nonpolymerizable actin mutant, placing actin downstream of mDia in
the signal pathway. The SRF activation assay was used to identify
inactive mDia1 derivatives that inhibit serum- and LPA-induced
signaling to SRF. We show that these interfering mutants also block
F-actin assembly, whether induced by mDia proteins or extracellular
signals. These results identify novel functional elements of mDia1 and
show that it regulates SRF activity by inducing depletion of the
cellular pool of G-actin.
Cancer Research UK, London Research Institute,
Lincoln's Inn Fields Laboratories, Transcription Laboratory, London
WC2A 3PX, United Kingdom
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