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J Biol Chem, Vol. 273, Issue 40, 25602-25611, October 2, 1998
From Dynamique du Cytosquelette, Laboratoire d'Enzymologie et
Biochimie Structurales, CNRS, 91198 Gif-sur-Yvette, France
The mechanism of control of the steady state of
actin assembly by actin depolymerizing factor (ADF)/cofilin and
profilin has been investigated. Using T
4 as an
indicator of the concentration of ATP-G-actin, we show that ADF
increases the concentration of ATP-G-actin at steady state. The
measured higher concentration of ATP-G-actin is quantitatively
consistent with the increase in treadmilling, caused by the large
increase in the rate of depolymerization from the pointed ends induced
by ADF (Carlier, M.-F., Laurent, V., Santolini, J., Didry, D., Melki,
R., Xia, G.-X., Hong, Y., Chua, N.-H., and Pantaloni, D. (1997)
J. Cell Biol. 136, 1307-1322). Experiments
demonstrate that profilin synergizes with ADF to further enhance the
turnover of actin filaments up to a value 125-fold higher than in pure
F-actin solutions. Profilin and ADF act at the two ends of filaments in
a complementary fashion to increase the processivity of treadmilling.
Using the capping protein CapZ, we show that ADF increases the number
of filaments at steady state by 1.3-fold, which cannot account for the
25-fold increase in turnover rate. Computer modeling of the combined
actions of ADF and profilin on the dynamics of actin filaments using
experimentally determined rate constants generates a distribution of
the different actin species at steady state, which is in quantitative
agreement with the data.
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