[HTML][HTML] Dissecting requirements for auto-inhibition of actin nucleation by the formin, mDia1
F Li, HN Higgs - Journal of Biological Chemistry, 2005 - ASBMB
The mammalian formin, mDia1, is an actin nucleation factor. Experiments in cells and in vitro
show that the N-terminal region potently inhibits nucleation by the formin homology 2 (FH2)
domain-containing C terminus and that RhoA binding to the N terminus partially relieves this
inhibition. Cellular experiments suggest that potent inhibition depends upon the presence of
the diaphanous auto-regulatory domain (DAD) C-terminal to FH2. In this study, we examine
in detail the N-terminal and C-terminal regions required for this inhibition and for RhoA relief …
show that the N-terminal region potently inhibits nucleation by the formin homology 2 (FH2)
domain-containing C terminus and that RhoA binding to the N terminus partially relieves this
inhibition. Cellular experiments suggest that potent inhibition depends upon the presence of
the diaphanous auto-regulatory domain (DAD) C-terminal to FH2. In this study, we examine
in detail the N-terminal and C-terminal regions required for this inhibition and for RhoA relief …
